\r\n\tRecycling is the collection and processing of items that would otherwise be discarded as waste in order to create a new product. Recycled material is being used in an increasing number of today's products. Waste management is primarily concerned with a wide range of wastes, including industrial, biological, household, municipal, organic, biomedical, and radioactive wastes. Human activity, such as the mining and processing of basic resources, generates waste and poses health problems that can emerge both indirectly and directly. Waste mismanagement is a serious problem on an individual and a governmental level. Nowadays, the waste disposal business is both hazy and straining to adapt to globalized consumerism, a system in which things are manufactured on one continent, purchased and used on another, and disposed of on still another. Therefore, remediation is often subject to a variety of legal criteria, but it can also be based on evaluations of human health and environmental concerns in cases where no statutory standards exist or when standards are advisory.
",isbn:"978-1-83768-012-2",printIsbn:"978-1-83768-011-5",pdfIsbn:"978-1-83768-013-9",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,isSalesforceBook:!1,hash:"64225f6a25b30e3652c70f464d810f34",bookSignature:"Prof. Hosam Saleh and Prof. Amal I. Hassan",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/12044.jpg",keywords:"Municipal Waste, Waste Management, Monitoring Systems, Biodegradable Waste, Industrialization, Industrial Wastewater, Pollutants, Innovative Technologies, Nuclear Waste, Hazardous Materials, Intrinsically Radioactive, Decontamination",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 10th 2022",dateEndSecondStepPublish:"June 7th 2022",dateEndThirdStepPublish:"August 6th 2022",dateEndFourthStepPublish:"October 25th 2022",dateEndFifthStepPublish:"December 24th 2022",remainingDaysToSecondStep:"20 days",secondStepPassed:!1,currentStepOfPublishingProcess:2,editedByType:null,kuFlag:!1,biosketch:"Hosam Saleh is a Professor of Radioactive Waste Management at the Radioisotope Department and a pioneering researcher in waste management, appointed head of Radioisotope Department, Egyptian Atomic Energy Authority. He was awarded an MSc and Ph.D. in Physical Chemistry from Cairo University. He is selected among the top 2% of scientists in the world according to the Stanford University report for 2020 and 2021.",coeditorOneBiosketch:"Amal I. Hassan is a Professor of Animal Physiology, Department of Radioisotopes, Nuclear Research Center, Atomic Energy Authority, Egypt. She has authored many peer-reviewed papers on chronic disease problems. She is a referee, reviewer, and editorial board member for several international scientific journals. She received a Certificate of Excellence in international scientific research arbitration from Publons. She was also selected for inclusion in Who’s Who in 2014, 2015, and 2016.",coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"144691",title:"Prof.",name:"Hosam",middleName:null,surname:"Saleh",slug:"hosam-saleh",fullName:"Hosam Saleh",profilePictureURL:"https://mts.intechopen.com/storage/users/144691/images/system/144691.png",biography:"Hosam Saleh is a Professor of Radioactive Waste Management at the Radioisotope Department, Atomic Energy Authority, Egypt. He was awarded with an MSc and PhD in Physical Chemistry from Cairo University. Saleh has more than 25 years of experience in hazardous waste management with an emphasis on treatment and developing new matrixes for immobilization of these wastes. He is also interested in studying innovative economic and environment-friendly techniques for the management of hazardous and radioactive wastes. He authored many peer-reviewed scientific papers and chapters and served as an editor of several books. He has been selected among the top 2% of scientists in the world according to the Stanford University report for 2020 and 2021.",institutionString:"Egyptian Atomic Energy Authority",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"13",totalChapterViews:"0",totalEditedBooks:"13",institution:{name:"Egyptian Atomic Energy Authority",institutionURL:null,country:{name:"Egypt"}}}],coeditorOne:{id:"218811",title:"Prof.",name:"Amal I.",middleName:null,surname:"Hassan",slug:"amal-i.-hassan",fullName:"Amal I. Hassan",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSEhMQAW/Profile_Picture_1634019809906",biography:"Dr. Amal I. Hassan is a Professor of Physiology at Department of Radioisotopes, Nuclear Research Centre, Atomic Energy Authority. She participated in a lot of research to find solutions to some chronic disease problems and she supervised some masters and doctoral theses. She is a referee and publisher\r\nmember of several international scientific journals. Dr Hassan is also a member of Publication Integrity and Ethics (PIE) in London. She obtained a Certificate of Excellence in the field of international scientific research\r\nreviewers from Publons. She was selected in the global encyclopedia (Who's Who Edition 31 for 2014, 32 for\r\n2015, and 33 for 2016).",institutionString:"National Research Centre",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"National Research Centre",institutionURL:null,country:{name:"Egypt"}}},coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"11",title:"Engineering",slug:"engineering"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"453623",firstName:"Silvia",lastName:"Sabo",middleName:null,title:"Mrs.",imageUrl:"https://mts.intechopen.com/storage/users/453623/images/20396_n.jpg",email:"silvia@intechopen.com",biography:null}},relatedBooks:[{type:"book",id:"10198",title:"Response Surface Methodology in Engineering Science",subtitle:null,isOpenForSubmission:!1,hash:"1942bec30d40572f519327ca7a6d7aae",slug:"response-surface-methodology-in-engineering-science",bookSignature:"Palanikumar Kayaroganam",coverURL:"https://cdn.intechopen.com/books/images_new/10198.jpg",editedByType:"Edited by",editors:[{id:"321730",title:"Prof.",name:"Palanikumar",surname:"Kayaroganam",slug:"palanikumar-kayaroganam",fullName:"Palanikumar Kayaroganam"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1591",title:"Infrared Spectroscopy",subtitle:"Materials Science, Engineering and Technology",isOpenForSubmission:!1,hash:"99b4b7b71a8caeb693ed762b40b017f4",slug:"infrared-spectroscopy-materials-science-engineering-and-technology",bookSignature:"Theophile Theophanides",coverURL:"https://cdn.intechopen.com/books/images_new/1591.jpg",editedByType:"Edited by",editors:[{id:"37194",title:"Dr.",name:"Theophile",surname:"Theophanides",slug:"theophile-theophanides",fullName:"Theophile Theophanides"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3161",title:"Frontiers in Guided Wave Optics and Optoelectronics",subtitle:null,isOpenForSubmission:!1,hash:"deb44e9c99f82bbce1083abea743146c",slug:"frontiers-in-guided-wave-optics-and-optoelectronics",bookSignature:"Bishnu Pal",coverURL:"https://cdn.intechopen.com/books/images_new/3161.jpg",editedByType:"Edited by",editors:[{id:"4782",title:"Prof.",name:"Bishnu",surname:"Pal",slug:"bishnu-pal",fullName:"Bishnu Pal"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3092",title:"Anopheles mosquitoes",subtitle:"New insights into malaria vectors",isOpenForSubmission:!1,hash:"c9e622485316d5e296288bf24d2b0d64",slug:"anopheles-mosquitoes-new-insights-into-malaria-vectors",bookSignature:"Sylvie Manguin",coverURL:"https://cdn.intechopen.com/books/images_new/3092.jpg",editedByType:"Edited by",editors:[{id:"50017",title:"Prof.",name:"Sylvie",surname:"Manguin",slug:"sylvie-manguin",fullName:"Sylvie Manguin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"371",title:"Abiotic Stress in Plants",subtitle:"Mechanisms and Adaptations",isOpenForSubmission:!1,hash:"588466f487e307619849d72389178a74",slug:"abiotic-stress-in-plants-mechanisms-and-adaptations",bookSignature:"Arun Shanker and B. Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"72",title:"Ionic Liquids",subtitle:"Theory, Properties, New Approaches",isOpenForSubmission:!1,hash:"d94ffa3cfa10505e3b1d676d46fcd3f5",slug:"ionic-liquids-theory-properties-new-approaches",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/72.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"314",title:"Regenerative Medicine and Tissue Engineering",subtitle:"Cells and Biomaterials",isOpenForSubmission:!1,hash:"bb67e80e480c86bb8315458012d65686",slug:"regenerative-medicine-and-tissue-engineering-cells-and-biomaterials",bookSignature:"Daniel Eberli",coverURL:"https://cdn.intechopen.com/books/images_new/314.jpg",editedByType:"Edited by",editors:[{id:"6495",title:"Dr.",name:"Daniel",surname:"Eberli",slug:"daniel-eberli",fullName:"Daniel Eberli"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"57",title:"Physics and Applications of Graphene",subtitle:"Experiments",isOpenForSubmission:!1,hash:"0e6622a71cf4f02f45bfdd5691e1189a",slug:"physics-and-applications-of-graphene-experiments",bookSignature:"Sergey Mikhailov",coverURL:"https://cdn.intechopen.com/books/images_new/57.jpg",editedByType:"Edited by",editors:[{id:"16042",title:"Dr.",name:"Sergey",surname:"Mikhailov",slug:"sergey-mikhailov",fullName:"Sergey Mikhailov"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1373",title:"Ionic Liquids",subtitle:"Applications and Perspectives",isOpenForSubmission:!1,hash:"5e9ae5ae9167cde4b344e499a792c41c",slug:"ionic-liquids-applications-and-perspectives",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/1373.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"2270",title:"Fourier Transform",subtitle:"Materials Analysis",isOpenForSubmission:!1,hash:"5e094b066da527193e878e160b4772af",slug:"fourier-transform-materials-analysis",bookSignature:"Salih Mohammed Salih",coverURL:"https://cdn.intechopen.com/books/images_new/2270.jpg",editedByType:"Edited by",editors:[{id:"111691",title:"Dr.Ing.",name:"Salih",surname:"Salih",slug:"salih-salih",fullName:"Salih Salih"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"57582",title:"Protein Kinases and Regulation of Mitochondrial Function in Ischemia/Reperfusion Injury",doi:"10.5772/intechopen.71094",slug:"protein-kinases-and-regulation-of-mitochondrial-function-in-ischemia-reperfusion-injury",body:'\nIschemia (insufficient oxygen and nutrient supply to an organ) can affect all major organs and is often encountered in many clinical and nonclinical settings including myocardial infarction, stroke, pulmonary embolism, major surgery, tissue trauma and hemorrhage, transplantation and organ storage, or hypotension in septic shock. Functional deficits caused by ischemia in major organs result in significant morbidity, disability, and mortality. Mitochondria are double-membrane-bound, dynamic organelles present in most eukaryotic cell types. They require large amounts of oxygen to generate ~90–95% of the total energy in oxidative phosphorylation occurring in a majority of cells [1]. Therefore, mitochondria are the key subcellular targets of ischemia, which undergo pathological changes that trigger cellular and tissue damage when oxygen is unavailable. Mitochondria perform several major cellular functions including energy and intermediary metabolisms, several biosyntheses, regulation of calcium storage, and redox homeostasis [1]. They are also involved in signaling, cell cycle, growth, differentiation, and cell death by apoptosis [2].
\nProteins of the mitochondrial electron transport chain and oxidative phosphorylation are among the primary targets of ischemia and oxidative stress during reperfusion [3]. Decreases in activities of adenine nucleotide translocase (ANT) and ATP synthase are among the earliest events after the onset of cardiac ischemia [4, 5, 6, 7]. Inhibition of NADH:ubiquinone dehydrogenase (complex I) and reduced cytochrome c content occur early during ischemia [5, 8], whereas the damage to ubiquinol:cytochrome c oxidoreductase (complex III) and cytochrome oxidase (complex IV) occurs in prolonged ischemia [5, 8]. Reduced activity of complex I is primarily caused by decreases in NADH dehydrogenase activity [5, 9] due to, in part, oxidative damage to the flavin mononucleotide (FMN) prosthetic groups, which results in electron leakage, superoxide production, and the generation of reactive oxygen species (ROS) in ischemic tissues [5, 10]. Ischemia decreases the activity of complex III by inactivating the iron-sulfur center, which contributes to electron leakage and superoxide production, and exacerbates oxidative stress originating from complex I [11]. The voltage-dependent anion channel (VDAC) and proteins of the mitochondrial permeability transition (MPT) pore are also targeted by I/R, which disrupts the transport of ions and solutes and the membrane potential for ATP synthesis [12, 13].
\nMitochondria are dynamic organelles that regularly undergo fission (fragmentation) and fusion (formation of a network of mitochondria) [14]. Fission is mediated by the dynamin-related protein 1 (Drp1) and mitochondrial fission protein 1 (Fis1) [14]. Fusion is regulated by the mitofusins (Mfn1 and Mfn2) and the optic atrophy protein 1 (Opa1) [14]. Drp1 and Opa1 are rapidly activated and translocated to mitochondria after ischemia in major organs. This promotes fission, the permeabilization of the mitochondrial outer membrane, and the release of proteins that initiate the intrinsic cascade of apoptosis [15, 16]. Inhibition of Drp1 inhibits fission and reduces cardiomyocyte death, the size of myocardial infarct, and acute kidney injury after ischemia [17]. Mitochondria also regulate the intrinsic cascade of apoptosis, which is activated after the release of mitochondrial proteins. Therefore, preservation of mitochondrial integrity and function is crucial for organ protection against I/R injury.
\nNumerous mitochondrial proteins (354 reported to date) are phosphoproteins that collectively contain 899 identified and 479 potential novel phosphorylation sites [18, 19]. Consequently, phosphorylation of mitochondrial proteins has emerged as an important mechanism involved in progressive damage of mitochondria in response to metabolic stresses including I/R and the status of these phosphorylations is key to understanding the regulation of mitochondrial functions in disease states [18, 19]. A number of protein kinases localize to mitochondria in response to I/R [19, 20]. Protein phosphorylations by these kinases produce differential outcomes in different tissues depending on the phosphorylation site and the kinase involved. The key proteins of oxidative phosphorylation, TCA cycle, transport, and the cascade of intrinsic apoptosis are regulated by phosphorylation [19, 20, 21, 22, 23].
\n\nDysfunction of complex I is the most common disorder of oxidative phosphorylation in humans. It is often due to defects of the subunit assembly to form the mature complex I. Complex I is a major mitochondrial target of I/R. Its activity decreases as early as 10 minutes into cardiac ischemia [24]. Our studies demonstrated that the activity of complex I in renal cortical mitochondria is decreased after renal ischemia [25]. Changes in the activity of complex I during I/R are also regulated by phosphorylation [4, 26]. Phosphorylations occur on several subunits of complex I. The NDUFA10 subunit is phosphorylated on S59 and S95 [27]. The NDUFS4 and NDUFA10 subunits are phosphorylated by mitochondrial protein kinase A (PKA), which stimulates the activity of complex I [27, 28, 29]. Phosphorylations of subunit ESSS on S20 and subunit MWFE (NDUFA1) on S55 regulate complex I assembly. Blocking these phosphorylations inhibits assembly of subunits to form a mature complex I and reduces its activity [26, 30]. Tyrosine phosphorylation of the NDUFB10 subunit by Src kinases also increases the activity of complex I, possibly by increasing its affinity toward NADH or increasing assembly of subunits into the fully active complex I [31, 32]. The reduced assembly of subunits leads to decreased levels of complex I [32]. This adaptation shifts fuel utilization from fuels that generate primarily NADH (carbohydrates) to fuels generating more FADH2 (fatty acids) oxidized by complex II. This shift may occur during nutritional restriction or after ischemic injury [32]. Further, complex I is primarily assembled into mitochondrial super-complexes, which increases O2 consumption and reduces ROS production [33]. Cardiac I/R induces disintegration of mitochondrial super-complexes, which reduces activity of the electron transport chain [34]. Thus, phosphorylation controls the formation, stability, and function of complex I and its assembly into super-complexes.
\nComplex II is an essential regulator of metabolic reprogramming and respiratory adaptation. Mitochondrial Src-type tyrosine kinase Fgr phosphorylates complex II on Y535, Y596, and Y604 when activated by ROS generated by I/R [32]. Phosphorylation of Y604 on the flavoprotein subunit of succinate dehydrogenase (FpSDH) increases activity of complex II and serves as a metabolic adaptation to increased ROS production [32, 34]. Fgr-mediated phosphorylation also reduces the protein levels of complex I, which alters the mitochondrial preference for fuel oxidation from NADH to FADH2, which increases the metabolic capacity of mitochondria to utilize alternative fuels when complex I is impaired [32]. Blocking phosphorylation of FpSDH on Y604 abolishes the capacity of mitochondria to adapt their metabolism after hypoxia/reoxygenation [32]. Mitochondrial phosphatases dephosphorylate Y604 and reverse this metabolic adaptation [32, 34]. In contrast, phosphorylation of FpSDH in cancer cells undergoing hypoxia decreases and dephosphorylation of FpSDH increases SDH activity [35]. Our data show that the activity of complex II in injured renal proximal tubular cells (RPTC) and in the ischemic kidney cortex is unchanged, whereas the activity of complex I is decreased [25, 36]. Supplementing the RPTC with succinate (complex II substrate) ameliorates mitochondrial dysfunction, ATP deficits, oxidative stress, and cell death after injury associated with the generation of ROS and oxidative stress [36].
\nPhosphorylation has been implicated in the regulation of the Rieske iron-sulfur protein of complex III, which is a major target of ischemia and the decreases in its activity lead to increased superoxide production [37]. Several phosphorylation sites have been identified on the subunits of complex III. The tyrosines on the core subunit 1 of complex III are phosphorylated by the Src kinase family, but the functional consequence of this phosphorylation is not yet known [38]. The role of phosphorylation of Rieske iron-sulfur protein is not clear and it was suggested that it regulates the MPTP opening [37].
\nTo date, 14 phosphorylation sites have been mapped on complex IV [39]. Tyrosine phosphorylation of the specific subunits of complex IV can lead to both inhibition and activation of complex IV activity [39, 40]. Bender and Kadenbach have shown phosphorylation of complex IV subunits I, II/III, and Vb
Phosphorylations of serine, threonine, and 2 tyrosine residues have been mapped on cytochrome c [39, 47]. Phosphorylation of T28 results in a partial inhibition of the electron transport chain and respiration [48]. It was suggested that the other phosphorylations regulate the mobility of cytochrome c between complexes, its binding to cardiolipin, and the interaction with Apaf-1 during apoptosis [47].
\nMultiple and differential phosphorylations of ATP synthase have been reported in different organisms and tissues. Tyrosine phosphorylations of the ε-subunit (in the Fo domain) and the α- and δ-subunits of the F1 domain are mediated by Src kinase [49, 50]. The α and e subunits of FoF1-ATPase in mammalian brain are phosphorylated on S76 and Y32 [51]. The catalytic β-subunit is extensively phosphorylated on S106, T107, T262/S263, T312, and T368 in mammalian cardiomyocytes, whereas in yeast, the β-subunit is phosphorylated on T58, S213, T262, and T318 [51]. These phosphorylations affect assembly of the F1 domain and reduce ATP synthase activity [51]. They occur in cardiac preconditioning, which offers protection against ischemia [51]. Phosphorylation of T213 on the β-subunit of skeletal muscle FoF1-ATPase downregulates its levels
ANT, an antiporter embedded in the inner mitochondrial membrane that facilitates the exchange of ADP and ATP, is one of the most abundant mitochondrial proteins and a primary target of ischemia [5, 53]. The four human isoforms, ANT1, 2, 3, and 4, are phosphorylated on tyrosines [49]. Phosphorylation of ANT on Y194 and Y190 alters the activity of ADP/ATP translocase and the transport of both nucleotides in the brain [49]. Phosphorylation of ANT1 at Y194 in cardiac tissue is diminished by I/R but maintained by pre- and post-conditioning, which suggests that this phosphorylation plays a protective role against ischemia in the heart and could improve tolerance against injury [54]. Although this phosphorylation improves respiration and mitochondrial function, it is not known whether phosphorylation of Y194 is sufficient for protection of cardiomyocytes from I/R-induced injury [54]. A binding of phosphorylated (inactive) glycogen synthase kinase-3β (GSK-3β) to ANT was also shown, but it is unclear whether GSK-3β directly phosphorylates ANT [55].
\nVDAC, a channel protein localized to the outer mitochondrial membrane, conducts a variety of small metabolites (NAD+/NADH, ADP, and ATP) and ions across the outer membrane and is a key regulator of energy metabolism [56]. VDAC forms a complex with ANT, which facilitates influx of ADP into mitochondria and the efflux of ATP to the cytoplasm [56, 57, 58]. VDAC1 closure leads to hyperpolarization of mitochondria, disruption of ADP/ATP exchange, decrease in ATP synthesis, and metabolic dysfunction, and rupture of mitochondria [56, 57, 58]. The four known VDAC isoforms present in the outer mitochondrial membrane are phosphorylated on multiple serines and threonines [21, 22]. A total of 19 distinct phosphorylations were identified in VDAC isoforms [21, 65]. These phosphorylations are mediated by different kinases including PKA, PKC, tyrosine kinase, hexokinase, GSK-3β, Akt, JNK3, and p38 [59]. The phosphorylation of neuronal and hepatic VDAC1 by PKA and ischemia-activated GSK-3β and JNK induces its closure, disrupts formation of the complex with ANT, and decreases ATP synthesis [59]. In contrast, phosphorylation of cardiac VDAC1 by protein kinase C-ε (PKC-ε) promotes formation of the VDAC-ANT complex, prevents the opening of MPTP, and protects mitochondrial integrity after I/R injury [60]. Phosphorylation of VDAC1 by never-in-mitosis A related kinase 1 (Nek1) on S193 closes the channel in RPTC, blocks release of cytochrome c, and prevents cell death by apoptosis [61]
\nPhosphoproteomic analyses revealed that most enzymes of the TCA cycle are phosphorylated/dephosphorylated [62]. These include aconitase, isocitrate and oxo-ketoglutarate dehydrogenases, succinyl-coenzyme A synthetase, succinate dehydrogenase, fumarate hydratase, and mitochondrial malate dehydrogenase [62, 63]. Although the functional role of these phosphorylations and the protein kinases that mediate them are not yet known, data suggest that phosphorylation regulates the activity of these enzymes.
\nPDC is composed of multiple copies of three distinct enzymes: (1) pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3), which form a large complex. PDC is the rate-limiting enzyme in the oxidative metabolism of all carbohydrates and its activity is tightly regulated by multiple mechanisms including phosphorylation. Phosphorylation of the PDC by the pyruvate dehydrogenase kinase (PDK) inactivates the complex [64]. The α-subunit of the E1 is phosphorylated at multiple sites, but the most known are phosphorylations of three distinct serines [64]. Although phosphorylation at any of these serines is sufficient to inhibit the activity of PDC, the S293 residue has the highest affinity for phosphate, and phosphorylation of this serine has the greatest impact on the inhibition of activity of PDC [64, 65]. I/R-induced injury in cardiac tissue is associated with a 4–5-fold decrease in the phosphorylation of S293, which results in the activation of PDC [64]. PDC activation protects against ischemic injury and improves cardiac efficiency and contractile capacity in the postischemic heart [65].
\nMitochondrial morphology is dynamically changed by the balance between fusion and fission (fragmentation). Phosphorylations of GTPases, Drp1, Mfn1/2, and Opa1 regulate mitochondrial fission and fusion [66]. Phosphorylation of fission-inducing Drp1 on S616 and S637 can be mediated by cyclin-dependent kinase (cdk)-1, cdk-5, PKA, PKC-δ, and extracellular signal regulated kinase-2 (ERK-2) [66, 67, 68, 69, 70, 71]. Phosphorylation of Drp1 at S616 by cdk-1, PKC-δ, and ERK-2 promotes Drp1 translocation to mitochondria and fission whereas phosphorylation of S637 by PKA inhibits Drp1 and mitochondrial fission [67, 68, 69, 70, 71]. We have demonstrated that activation of PKC-ε induces the translocation of Drp1 to mitochondria, mitochondrial fission and apoptosis in non-injured RPTC [72]. Drp1-dependent mitochondrial fission is associated with mitochondrial outer membrane permeabilization and apoptosis, whereas elongation of the mitochondria through fusion promotes ATP synthesis and prevents mitochondrial autophagy. When phosphorylated by ERK, Mfn1 has decreased ability to oligomerize and tether mitochondria, which inhibits their fusion, recruitment of Bak to the mitochondria, and apoptosis [73]. Mfn2 is phosphorylated on T111 and S442 by PTEN-induced putative kinase protein 1 (PINK1), which recruits the protein Parkin to depolarized mitochondria and eliminates them by mitophagy [74]. Disruption in the balance between fission and fusion occurs in pathological conditions including I/R, which increases phosphorylation of Drp1, its translocation to mitochondria, and mitochondrial fission in the heart and brain [75]. Inhibition of Drp1 protects the heart and brain against ischemia and has been proposed as a therapeutic target following cardiac arrest [76].
\nMitochondrial proteins involved in the intrinsic apoptosis include Bcl-2 family members, AIF, Smac/DIABLO, cytochrome c, and Omi/Htra2. With an exception of one, all are regulated by phosphorylation [20]. Phosphorylation of Bcl-2 at S70 is required to prevent permeabilization of the mitochondrial outer membrane and for Bcl-2’s anti-apoptotic activity [77]. Several protein kinases serve as Bcl-2 kinases to inhibit (JNK, p38, and GSK-3) or activate (Akt, PKA, and PKC-α) Bcl-2 [77]. Cardiac and neuronal tissues are protected against I/R when Bcl-2 is active [78, 79, 80]. Ischemia-induced acute kidney injury upregulates Bcl-2 and Bcl-XL in the distal and Bax in the proximal tubules [80]. Pro-apoptotic Bax, Bak, Bad, and Bid are phosphorylated on serines and tyrosines, which controls their insertion into the outer mitochondrial membrane and formation of pores that mediate the release of pro-apoptotic AIF, Smac, and cytochrome c from the mitochondria [81]. Smac is phosphorylated by JNK3, which decreases its pro-apoptotic actions [81]. Phosphorylation of Y97 and Y48 on cytochrome c regulates its capacity to form the apoptosome and activate caspase-9 [81]. Thus, phosphorylation of specific amino acids on a mitochondrial protein determines the fate of mitochondria by protecting their integrity and functions or inducing MPT and apoptosis.
\nIschemia rapidly changes activities of different protein kinases including the calcium/calmodulin-dependent protein kinase II (CaMK-II), PKA, protein kinase B (PKB/Akt), PKC, Raf-1, ERK1/2, c-jun N-terminal kinase (JNK), p38 mitogen-activated protein kinase (p38 MAPK), GSK3-β, PINK1, and tyrosine kinases, which suggests their involvement in I/R injury.
\nA specific family of protein kinases is exclusively present in the mitochondrial matrix of eukaryotic cells. These kinases have different sequences from the cytosolic protein kinases and they phosphorylate and inactivate large enzymatic complexes in the mitochondrial matrix, the branched-chain α-ketoacid dehydrogenase complex and pyruvate dehydrogenase complex, PDC. Perturbations in PDC activity result in energy deficits, neuronal dysfunction, and brain injury, such as those observed in stroke. Phosphorylation of the E1 α-subunit of PDC by PDK isozymes inhibits, whereas dephosphorylation increases PDC activity [82]. Cardiac and cerebral ischemia has no effect on the activity of PDC; however, reperfusion results in a fast decline in PDC activity in the brain [83]. Increased expression of PDK2 following traumatic brain injury may maintain E1 in the hyperphosphorylated (inactive) state, which impairs glucose oxidation after stroke and traumatic brain injuries [83]. Further, reperfusion-induced oxidative stress activates PKC-δ, which translocates to mitochondria and activates PDK2 leading to inhibition of E1 activity [84]. The inhibition of PDK during reperfusion restores PDC activity and decreases brain injury, demonstrating that phosphorylation by PDK2 mediates inhibition of PDC activity [85]. Infusion of the specific peptide inhibitor of PKC-δ, Tat-δV1-1, prevents the translocation of PKC-δ to mitochondria and maintains PDC activity [84]. Isozymes of PDK are considered attractive targets for therapies to improve PDC activity to diminish the detrimental effects of I/R in tissues that depend on metabolism of glucose, such as neuronal and cardiac tissues.
\nPKA is activated by a signaling pathway originating from G-protein receptors, which produces cAMP. The association of PKA with mammalian mitochondria was documented four decades ago [86]. Mitochondrial PKA is present in the outer and inner mitochondrial membranes as well as in the mitochondrial matrix [28, 87]. Several mitochondrial substrates of PKA with distinct tissue-specific responses have been identified. During myocardial I/R, PKA is activated by increased levels of ROS and translocates to mitochondria [88]. The increase in activity of mitochondrial PKA is independent of mitochondrial levels of cAMP and is due to increased sequestration of the catalytic α-subunit in the mitochondrial matrix [88]. The presence of the catalytic α-subunit of PKA results in phosphorylation of subunits I (on S115 and S116), IVi1 (on T52), and Vb (on S40) of complex IV, followed by their degradation and the loss of activity [38, 40, 88]. Because the identified phosphorylation sites on complex IV are not within PKA consensus sites, it was proposed that PKA activation plays an indirect role in the loss of complex IV activity during myocardial ischemia [39]. These changes are sufficient to disrupt the function of mitochondrial respirasome and increase production of ROS [88]. PKA-mediated phosphorylation regulates ischemia-induced dysfunction of complex IV [38, 45, 88]. Ca2+ influx activated by PKA in cardiomyocytes induces mitochondrial permeability transition, which stimulates caspase-9 and apoptosis [89]. Inhibition of PKA prevents the loss of activity of complex IV during cardiac I/R, promotes postischemic cardiac contractile recovery, and decreases the infarct size in the ischemic heart [38, 45, 90]. Thus, PKA inhibitors could serve as candidates for cardioprotective agents [87, 89]. PKA also phosphorylates NDUFS4 and NDUFA10 subunits of complex I and this phosphorylation stimulates the activity of complex I and complex I-driven respiration [28, 29, 91]. Finally, Hsp20, which localizes to mitochondria and is expressed at high levels in cardiac, skeletal, and vascular smooth muscle, is regulated by the β-adrenergic/PKA signaling pathway [92]. PKA-mediated phosphorylation of Hsp20 on S16 increases in ischaemic myocardium and is cardioprotective [92].
\nIn contrast, the activation of PKA during liver IR is cAMP-dependent and plays a protective role against liver injury [93]. The cAMP that activates mitochondrial PKA does not originate from membrane-bound adenylyl cyclase activated by the Gα protein, but is produced inside mitochondria by the carbon dioxide/bicarbonate-regulated soluble adenylyl cyclase in response to metabolically generated carbon dioxide [93]. Mitochondrial PKA regulates mitochondrial biogenesis, normalizes ROS production, and activates complex IV [46]. Inhibition of PKA exacerbates hepatocellular damage, whereas increasing cAMP levels to activate PKA protects the ischemic liver from injury [93]. PKA activation diminishes neutrophil and macrophage infiltration into ischemic liver tissue, reduces production of tumor necrosis factor α, interleukin (IL)-6, and IL-12 by macrophages, increases IL-10 expression, and prevents hepatocyte death [93]. Thus, PKA activation reduces the inflammatory response associated with reperfusion after liver ischemia. Because ischemia is an inherent component of liver transplantation, activation of PKA was proposed as a rationale for novel therapies to combat I/R injury and protect transplants [94]. However, increased cAMP levels in the liver
PKA dysregulation has been implicated in several neurodegenerative disorders. PKA-dependent pathways in different regions of the brain play a role in pathogenesis and cognitive decline in Alzheimer and Parkinson’s diseases [94]. The acute phase of cerebral ischemia is accompanied by decreases in affinity of PKA for cAMP and PKA activity [94]. In contrast, the peri-ischemic and less-injured areas exhibit increased PKA-mediated phosphorylation compared to the ischemic core, which suggests that active PKA is associated with the survival of neuronal tissue [94]. Derangement of cAMP-dependent signal transduction is associated with ischemic neuronal damage and activation of the PKA is important for neuronal survival in acute cerebral ischemia [94]. Phosphorylation of Bad at S155 by mitochondria-anchored PKA leads to cytosolic sequestration of Bad and blocks its mitochondrial translocation, the release of cytochrome c, and neuronal apoptosis [77]. Also, PKA-mediated phosphorylation of Drp1 at S637 blocks its translocation to mitochondria and their fission and promotes mitochondrial fusion. In hippocampal neurons, expression of a constitutively active catalytic subunit of PKA targeted to the mitochondrion promotes the fusion of mitochondria into networks [95]. Finally, PKA suppresses autophagy and mitochondrial degradation in neurons by phosphorylating and inhibiting the microtubule-associated protein 1A/1B-light chain 3 (LC3) and increases neurite outgrowth [94, 96].
\nAkt can localize to the mitochondrial matrix and the inner and outer membranes of cardiac, neuronal, and kidney cells [97, 98]. Protein levels of mitochondrial Akt are regulated by a variety of extracellular signals and stresses, which induce rapid translocation of active (phosphorylated) Akt to the mitochondria [97, 98]. Mitochondrial localization of Akt is associated with cardioprotection against ischemic injury and renoprotective actions against chemical toxicity [97, 98, 99, 100]. The cardioprotective effect of mitochondrial Akt is attributed to its action on mitoK(ATP) channels and to decreasing apoptosis [99]. Akt phosphorylates pro-apoptotic Bad on S136 and Bax on S184, and prevents MPT in neuronal cells [101]. Phosphorylated Bad associates with 14-3-3 proteins in the cytosol and cannot form complexes with mitochondrial Bcl-2/Bcl-XL to induce permeabilization of the mitochondrial outer membrane and MPT [101]. Bax phosphorylation by Akt promotes dimerization of Bax with Bcl-XL or Mcl-1 proteins, which sequesters Bax away from mitochondria and prevents their permeabilization and apoptosis [101]. Akt prevents the MPT in cardiomyocytes by phosphorylating hexokinase II, stabilizing it in the outer mitochondrial membrane, and promoting its binding to VDAC [102]. Inhibition of Akt or targeted disruption of the association of hexokinase II with mitochondria abolishes cardioprotection [102].
\nWe have identified mitochondria as a subcellular target of protective actions of Akt against necrosis in injured RPTC [98]. Mitochondrial levels of active Akt decrease in injured RPTC and this is associated with mitochondrial dysfunction [98, 100]. Selective activation of Akt increases the levels of Akt in mitochondria, improves state 3 respiration, activities of complexes I and III and F0F1-ATPase (ATP synthase), and the mitochondrial membrane potential (ΔΨm), increases ATP production, and reduces ATP deficits [100]. Selective inhibition of Akt exacerbates mitochondrial dysfunction, energy deficits, and necrosis in injured RPTC [100]. These results are consistent with a report that Akt phosphorylates the β-subunit of ATP synthase and improves its activity and increases ATP production to prevent energy deficits in injured cells [97]. Also, active Akt increases activity of PDC and oxidative metabolism of carbohydrates by inhibiting phosphorylation of PDC by GSK-3β [103]. Thus, signals from cell membrane receptors or those generated by metabolic stress have a rapid effect on Akt activation status in mitochondria. Akt could serve as a therapeutic target promoting mitochondrial functions in ischemic organs. However, the application is complicated by the fact that Akt promotes tumor formation by blocking apoptosis.
\nPKC plays a key role in mediating I/R injury in the brain, heart, and kidneys; however, elucidation of this role is complicated due to the presence of 11 distinct PKC isozymes, which have unique tissue and cellular localizations and often play quite opposite roles in ischemic injury even within the same organ. Alterations in PKC activity or subcellular localization during ischemia occur in the brain, heart, liver, and kidney [25, 104, 105, 106]. Major isozymes of PKC (α, β, γ, δ, ε) translocate to mitochondria in response to ischemia and/or reperfusion and oxidative stress, and have been implicated in regulating mitochondrial functions in ischemic and postischemic tissues [104]. The classical PKC isozymes (α, β, γ) are dependent on Ca2+ and 1,2-diacylglycerol, and ischemia increases the levels of both activators through the stimulation of phospholipase C. PKC-α activation has been implicated in ischemia-induced heart failure and cerebral barrier breakdown after ischemic stroke [107, 108]. PKC-α inhibition or deletion protects the heart from decompensation and cardiomyopathy and attenuates cerebral barrier breakdown after ischemia [107, 108]. In contrast, PKC-α translocation to mitochondria is protective against mitochondrial dysfunction, ATP deficits, and cell death caused by ischemia, hypoxia, and oxidative stress in RPTC [109]. We have shown that ATP synthase (F0F1-ATPase) is a target of PKC-α, which associates with the α-, β-, and γ-subunits of the F1 domain of ATP synthase [52]. Injury or inactive PKC-α disrupt, whereas active PKC-α promotes this association and increases the levels of α-, β-, and γ-subunits in injured RPTC [52]. Active PKC-α promotes phosphorylation of the γ-subunit on S146 and F0F1-ATPase activity after injury [52]. PKC-α also reduces apoptosis by phosphorylating mitochondrial Bcl-2 on S70 [77, 110]. Thus, activation of PKC-α exerts differential effects in different types of cells and tissues.
\nPKC-γ is expressed exclusively in neurons of the brain and spinal cord and is activated rapidly during ischemia and inhibited during reperfusion [111, 112, 113, 114]. PKC-γ plays a detrimental role in the early stages of ischemia mediating events leading to cell death. PKC-γ knockouts show smaller infarct areas after cerebral ischemia [112]. Also, PKC-γ may directly (or through the activation of a Src tyrosine kinase) phosphorylate NMDA receptors, stimulate their function, and increase the concentration of intracellular Ca2+, which results in mitochondrial dysfunction, ATP deficits, increased ROS formation, and neuronal death [112]. However, after reperfusion, PKC-γ may mediate protection against cell death [112]. Thus, the same PKC isozyme may play opposing roles at different stages of ischemic injury.
\nPKC-δ is rapidly activated by signaling initiated by reperfusion. PKC-δ plays a detrimental role in ischemic stroke injury and mediates oxidative stress, cell death, and inflammation associated with reperfusion [111, 112]. Selective inhibition or deletion of PKC-δ reduces infarct size and ischemic brain injury caused by middle cerebral artery occlusion, specifically, reperfusion-induced death of parenchymal cells [115, 116]. PKC-δ inhibition activates PKB/Akt, inhibits translocation of Bad to mitochondria, and decreases apoptosis [112]. PKC-δ mediates neutrophil infiltration, which is responsible for the detrimental effects of PKC-δ during reperfusion [112]. Similarly, reperfusion after cardiac ischemia activates PKC-δ, which translocates to mitochondria and reduces state 3 respiration, TCA cycle, and ATP production, increases generation of mitochondrial ROS, and induces release of cytochrome c and cell death [84, 113, 115, 116]. Selective inhibition of PKC-δ translocation to mitochondria blocks these changes and protects the heart from ischemic injury [117]. PKC-δ is also activated by oxidative stress in the kidney, exacerbates RPTC and kidney injury by activating Bax, inducing cytochrome c release and apoptosis, and blocking autophagy. PKC-δ inhibition protects kidneys from injury by upregulating autophagy [118].
\nPKC-ε, another novel isozyme, is activated and translocates to mitochondria during I/R. These events have been implicated in the cardio- and neuro-protection against ischemic injury and in the reduction of myocardial infarct [119, 120]. PKC-ε activation is a pivotal signaling event in the cardioprotective mechanisms of ischemic preconditioning, and it is thought that this protection is mediated through mitochondrial and transport mechanisms [120]. Conversely, inhibition of PKC-ε eliminates the cardioprotection [120]. Several substrates of PKC-ε are present in cardiac mitochondria. Active PKC-ε induces opening of the mitoK(ATP) channels, maintains ATP production, and reduces ROS production [120]. Specifically, PKC-ε regulates interactions between conexin43 and the mitoK(ATP) subunit, which leads to mitoK(ATP) opening when ATP levels decrease, resulting in cardioprotection [121]. Active PKC-ε also increases phosphorylation of subunit IV and the activity of complex IV [122]. Thus, the PKC-ε-mediated resistance to cardiac ischemia may also be due to increased activity of the electron transport chain and a greater ΔΨm for ATP synthesis. Also, PKC-ε phosphorylates VDAC1 on T51, which modifies its gating and interaction with proteins of the MPT pore to inhibit its opening and maintain ΔΨm and ATP synthesis [60]. These data support protective and prosurvival actions of mitochondrial PKC-ε in cardiac I/R. In contrast, translocation of the active PKC-ε to mitochondria in RPTC results in mitochondrial dysfunction, decreases in ATP levels, mitochondrial fission, and RPTC death [25, 72]. Active PKC-ε produces the classical hallmarks of mitochondrial dysfunction in RPTC: decreases in state 3 respiration and activity of complex I, increases in ΔΨm, ROS production, and mitochondrial fission [25, 72]. Inhibition of PKC-ε protects against mitochondrial dysfunction induced by hypoxia and oxidative stress [72]. Deletion of PKC-ε
ERK1/2 localize to the mitochondria of cardiac, brain, and renal epithelial cells. Brain and cardiac ischemia activates ERK1/2, which form signaling modules with PKC-ε and translocate to mitochondria [124, 125, 126]. ERK1/2–PKC-ε modules play a role in the phosphorylation and inactivation of Bad, which blocks the intrinsic pathway of apoptosis [126]. Furthermore, active ERK1/2 associates with the outer mitochondrial membrane and protects against MPTP opening and mitochondrial depolarization [127]. These events are thought to contribute to the cardioprotective effects of ERK1/2 activation against I/R injury. In contrast, ERK1/2 activation is detrimental to mitochondria and cell viability in RPTC [128]. We have shown that ERK1/2 activation and translocation to mitochondria in response to oxidant injury mediates mitochondrial dysfunction and cell death in RPTC [128]. ERK1/2 activation mediates decreases in state 3 respiration, activities of aconitase of the TCA cycle and complex I of the electron transport chain, and ATP production in injured RPTC [128]. ERK1/2 inhibition restores respiration, complex I activity, ΔΨm and ATP production, and decreases RPTC death [128]. Recently, it was shown that ERK1/2 downregulates mitochondrial function through the EGFR/ERK1/2/FOXO3a/1/PGC-1α pathway by phosphorylating the upstream regulators of PGC-1α and decreasing mitochondrial biogenesis [129]. Similarly, ERK1/2 activation mediates inflammatory changes, infiltration by neutrophils, apoptosis, and severe injury after ischemia in the lung [130].
\nJNK and p38 MAPK are activated and localize in cardiac mitochondria after ischemia or oxidant exposure and mediate mitochondria-initiated apoptosis [131]. p38 MAPK inhibition attenuates the loss of ΔΨm, mitochondrial swelling, and ultrastructural changes, reduces cardiomyocyte apoptosis and infarct size, and improves left ventricular function after ischemia [131, 132]. Inhibition of p38 MAPK also decreases phosphorylation of p53 and Bax expression and reduces cytochrome c release from mitochondria and the levels of active caspase 3 [132]. These data suggests that active p38 MAPK mediates apoptosis.
\nGSK3β activated by cardiac I/R docks to mitochondria, phosphorylates VDAC1, and leads to phosphorylation of ANT and cyclophilin D, and MPTP opening [55, 133]. This suggests that GSK3β plays a role in mitochondria-mediated apoptosis in cardiac tissue. GSK3β also regulates mitochondrial oxidative metabolism by phosphorylating and inhibiting PDC [65]. Activation enhances whereas inhibition of GSK3β activates mTOR pathway, inhibits mTOR-dependent autophagy, and reduces myocardial I/R injury [134]. Inhibition of GSK-3β also attenuates brain infarct volume after cerebral I/R-induced injury [135].
\nThe mitochondrial serine-threonine protein kinase, PTEN (phosphatase and tensin homolog on chromosome 10)-induced kinase 1 (PINK1) localizes to both mitochondrial membranes and regulates mitochondrial function and dynamics [136]. PINK1 phosphorylates mitofusin MFN2, a mitochondrial receptor for Parkin (a protein related to Parkinson’s disease) [136]. PINK1 regulates mitochondrial dynamics in ischemic stroke and prevents damage to neurons by reducing mitochondrial translocation of Drp1 and fission, and preventing the collapse of ΔΨm and ATP synthesis [137, 138]. Deletion of PINK1 causes defects in the turnover of proteins of the electron transport chain, impairs mitochondrial respiration and activity of complex I in cardiomyocytes, induces MPTP opening, decreases production of ATP, exacerbates oxidative stress, and increases the size of ischemic myocardial infarct, which suggests increased susceptibility to I/R injury in PINK1-deficient hearts [139]. Overexpressing PINK1 reduces these changes [139]. Thus, this study suggests mitochondrial PINK1 as a target for cardioprotection against ischemia in the heart.
\nTyrosine phosphorylation is a crucial mechanism for regulating mitochondrial functions [19, 42]. Tyrosine kinases of the Src family (Lyn, Lck, c-Src, Fyn, and Fgr) localize to mitochondria by binding to specific anchoring proteins present in mitochondria [19, 42]. The primary known role of tyrosine phosphorylation is the regulation of the respiratory chain by c-Src [19]. Phosphorylations of NDUFB10 subunit of complex I at Y193, succinate dehydrogenase of complex II at Y215, and subunit II of complex IV on unknown tyrosine by Src increase activities of complexes I, II, and IV [19, 31, 42]. Targeting of c-Src to mitochondria enhances ΔΨm and oxidative phosphorylation in a c-Src-dependent manner [19]. Src and Lck phosphorylate ANT1 at Y194 and reduce ischemic injury in preconditioned cardiac cells [54]. Mitochondrial Fgr kinase phosphorylates complex II, which increases complex II activity and regulates NADH/FADH2 balance in mitochondria [32]. Epidermal growth factor receptor (EGFR) translocates to mitochondria when phosphorylated on Y845 by Src [43]. EFR interacts with and phosphorylates subunit II of complex IV thereby decreasing its activity and cellular ATP levels [19, 140].
\nIn conclusions, translocation of protein kinases to mitochondria regulates mitochondrial functions in various disease states including ischemia and reperfusion in major organs such as the brain, heart, and kidneys. These findings suggest that these protein kinases can serve as potential effective therapeutic targets to maintain mitochondrial integrity and functions and prevent or reduce organ damage in these disease states.
\nPrebiotics and probiotics have been proven to confer multiple health benefits to animals and humans alike when consumed either singly or in combination. Consumption of prebiotics and probiotics modulates the gut microbiota and the colonization of the gastrointestinal tract which is now known as the second gene pool of the human body. Evidence shows the health benefits of synbiotic intake in many aspects of human health including metabolic functions, gastrointestinal diseases, and bone health. Some of these documented evidence-based benefits include their immunomodulatory effect [1], improvement of diarrhea, lactose metabolism, digestive health and metabolic syndrome [2], antidiabetic and hypocholestrolemic [3], anticarcinogenic [4] and hypotensive attributes/features [5]. In a short review that we conducted, the importance of prebiotics, probiotics and synbiotics was expressed to be important across human lifespan from childhood to adulthood and the elderly [6].
\nProbiotics in the presence of prebiotics undergo different biochemical pathways/messenger systems to inhibit pathogens and boost the immunity of the host, these includes
Presence of probiotics in the gut leads to competition for nutrients with pathogens which can then lead to starvation and reduction of these unwanted bacteria.
Probiotics tend to compete for space via the adhesion effect to the mucosal lining by directly decreasing the adhesion of the pathogens and their toxins; this has been confirmed by in vitro studies demonstrating that probiotics possess lectin-like adhesion properties capable of binding carbohydrates from the receptors of glycoconjugate of epithelial cell surface [7] which blocks pathogen binding to the epithelial cell surface. Some probiotic strains of the
Probiotics are responsible for the synthesis of bacteriocins such as lantibiotics (class I) and class II bacteriocins by the probiotics, and this mainly by lactic acid bacteria (LAB) can help prevent the growth, colonization, and establishment of pathogens in the gut environments. These bacteriocins present a better activity on the pathogens than antibiotics due to their narrow-spectrum activity on foreign unwanted bacteria. Bacteriocins from Gram-positive bacteria are composed of membrane peptides capable of targeting and causing apoptosis of the cell membrane; however, most antibiotics inhibit enzymes and biosynthesis pathway in cells such as DNA, RNA, protein and cell-wall synthesis [9].
Probiotic microorganisms may also be able to produce enzymes, such as lipase, esterase, and co-enzymes A, Q, NAD, and NADP [10]. Likewise, some of the by-products of probiotics’ metabolism may exhibit antibiotic properties and these include bacitracin, lactacin and acidophiline [11].
The bio-metabolization of prebiotics into lactate and short chain fatty acids (SCFAs) such as acetate, mainly produced by
The production of butyrate is mainly from complex carbohydrates through the pyruvate and acetyl-coenzyme A (CoA) pathway; however, it can also be produced from amino acids via the glutarate, 4-aminobutyrate and lysine pathways in the gut [13]. Butyrate acts epigenetically as histone deacetylase (HDAC) inhibitors and the research into HDAC may be capable of providing cancer chemoprevention and therapies [16]. There are different functions of butyrate in the colon; it is the main source of energy for colonocytes. Furthermore, butyrate has been documented to inhibit proinflammatory cytokines such as tumor necrosis α (TNF-α) in monocytes [17], interferon-α (IFN-α) and IL-2 in rat mesenteric lymph nodes [18], chemokine CXCL-8 (IL-8) in Caco-2 cells [19].
Intake of prebiotics and probiotics has been linked to the development of immunomodulatory capacity by decreasing inflammation, antibody response and phagocytosis. Probiotics may be involved in the prevention of cytokine-induced epithelial damage.
Probiotic and prebiotic intake results in the improvement of the epithelial barrier integrity by the secretion of mucin [21] and defensins [22] including antimicrobial proteins (AMPs). Probiotics enhance the mucosal integrity also by inducing cytoprotective substance production by enterocytes such as heat shock proteins [23]. In an in vitro study,
Prebiotics and probiotics are capable of the stimulation and production of antioxidant-related enzymes, systemic hormones, and neurochemicals such as serotonin, gamma-aminobutyric acid (GABA) and cortisol, as well as production of bile salt hydrolase. Consumption of probiotics and prebiotics has also been reported to be able to reduce cholesterol levels. Prebiotic fibers increased levels of satiety hormones (glucagon-like peptide-1, proglucagon and peptide YY mRNA) and decreased levels of ghrelin O-acyltransferase mRNA in rats [26]. Furthermore, prebiotic fermentation in the gut likewise improved satietogenic and incretin gut peptide production, thereby increasing the plasma glucagon-like peptide 1 and peptide YY concentrations in humans [27].
Prebiotics and probiotics are responsible for the synthesis of antigens via production of anti-inflammatory cytokine such as IL-10 which inhibits the T-helper cells (1, 2, 7 and 17) and transforming growth factor-β responsible for the production of immunoglobulin A [28].
The concept and use of prebiotics has been argued to be more important when compared to probiotics due to the vulnerability and susceptibility of probiotics to environmental stresses, manufacturing process (such as heat) and endangered conditions during storage [29].
\nGlenn Gibson and Marcel Roberfroid launched the prebiotic concept in 1995 as ‘a nondigestible food ingredient that beneficially affects the host by selectively stimulating the growth and/or activity of one or a limited number of bacteria in the colon, and thus improves host health’ [30]. This definition has however been modified several times, but the initial main features have been retained. Prebiotics tend to stimulate the growth of the gut bacteria endogenously. The pH of the gut environment plays a major role in determining bacterial interspecies competition outcome.
\nFood sources of prebiotics consist of edible plants such as fruits, vegetables, cereal component which provides the body with carbohydrate. Specific potential sources are artichokes, tomatoes, bananas, asparagus, garlic, berries, kiwi fruit, onions, chicory, green leafy vegetables, legumes as well as linseed, barley, oats, and wheat.
\nEven though various molecules can be prebiotics, the great majority are dietary fibers which are oligosaccharides such as inulin (mainly from chicory), GOS (obtained from lactose using β-galactosidase), Fructooligosaccharides (FOS) (from chicory by partial enzymatic hydrolysis), soybean oligosaccharides (SOS), and xylooligosaccharides (XOS). Inulin, GOS and FOS have been widely studied. The list of prebiotics also includes compounds such as resistant starches, arabinoxylan, pectin, whole grains as well as non-carbohydrate complex such as polyphenols [13]. Absence of dietary fiber in the colon causes anaerobic bacteria to obtain their energy from protein fermentation, and this metabolism leads to the production of potentially toxic and carcinogenic compounds such as ammoniac and phenolic compounds [31]. In contrast, carbohydrate fermentation (for example dietary fiber) will produce non-toxic SCFAs which can serve as fuel for the epithelial cells. The production of volatile fatty acids, including, SCFAs and BCFAs, play a role in energy homeostasis maintenance as well as in the regulation of functionality in peripheral tissues [32]. Prebiotics are also mainly active in the large intestine/colon.
\nDifferent strains of bacterial genus or species would prefer different substrates for fermentation in the colon. Generally, the strains of
The use of prebiotics has been shown to be efficient and effective against a few human health disorders such as Type 2 diabetes mellitus and inflammatory bowel diseases which has been termed the “Western” chronic diseases and colorectal cancer. This is accomplished by the modulation of the intestinal gut microbiota which confer a protective, metabolic, and trophic benefits to the host [13].
\nThe history of probiotics spans back to the 20th century when Mechnicoff (1907) revealed the virtues associated with the consumption of fermented dairy products, he hypothesized that the aging process resulted from the putrefaction of the large intestine. Almost simultaneously, another scientist Tissier indicated that the main component of the gut flora of breast-fed infants were bifidobacterial [35]. Even earlier, biblical recommendations have pointed out yoghurt as important/significant for the treatment of some ailments [36]. Furthermore, the indication has been that probiotics is more beneficial when consumed with food as opposed to supplement due to the available nutrient and energy sources. Probiotics are mainly active in the small and large intestine.
\nOrganizations such as FAO, WHO and the European Food Safety Authority have indicated probiotic strains must meet both safety and effectiveness criteria for their selection process. The regulations require that safety and absence of risks is paramount for human and animal health. The human probiotic products usually belong to the
Probiotic use has been postulated to be potent against human disorders such as inflammatory enteral diseases such as Crohn’s disease, colitis, and non-specific ileitis. Intake of probiotics has also been assessed by various studies as capable of treating lactose intolerance, irritable bowel syndrome [37] and in the prevention of peptic ulcers and colorectal cancer [38]. Beneficial effects of probiotics have been observed in the process of digestion, food allergies treatment [39], dental caries [40], and candidoses [41]. The beneficial effects of probiotics observed by the host through augmentation of the epithelial wall, intestinal mucosal and competitive elimination of pathogens has been reported to aid inflammatory bowel disease (determined by cytokine-induced harm to the epithelial cell walls). Probiotics is capable of repressing gut inflammation via the downregulation of Toll-like Receptors’ expression, the prevention of TNF-α entrance into the mononuclear cell in blood and the suppression of enterocyte’s NF-kB (Nuclear Factor kappa-light-chain-enhancer of activated B cells) signaling pathway [42].
\nSynbiotics are a combination of prebiotics and probiotics. The consumption and intake of the combination of prebiotics and probiotics has been reported to stimulate, modulate, and alter the gut microbiota by lowering the colonic secretion of pro-inflammatory and immunoregulatory cytokines such as TNF-α, IL-1β and IL-6. Synbiotics can be used to help improve the beneficial microbes as well as increase the number of specific beneficial strains in the gastrointestinal tract [11].
\nImmunomodulatory effects of prebiotics and probiotics on human health.
\nOne the putative ways by which prebiotics and probiotics affect the health is altering the immune system. There are two categories of the immune system: either the innate immunity or the adaptive immune system. The immune system is responsible for protecting the host against pathogens. The type of effective immune response which recognizes and mounts reactions to eliminate the pathogen is determined by the site and type of pathogen present. Prebiotics and probiotics modulate the gut immune system thereby also having effects on bone health.
\nFurther studies are needed to investigate the benefits of synbiotics on bone health both in human and animal model.
\nBone loss/osteoporosis is a major health problem that is associated with the imbalance between bone formation and bone resorption; often resulting in osteoporotic fractures. In addition, the estimation is that one in two women and one in four men over the age of 50 years will break a bone due to osteoporosis in their life time [43]. Postmenopausal osteoporosis is largely attributed to estrogen deficiency in women age 50 years and above due to ablation of the ovarian function which stimulates bone resorption resulting in bone loss. Risk factors leading to bone diseases include internal (genetic and aging) and external modifiable factors (e.g., diet, exercise, environment, medication etc). In osteoporosis treatment, different approaches have been used but lately due to the safety, low adverse effect and lack of major side effects, probiotics and prebiotics have been introduced. Treatment of bone diseases including osteoporosis and fracture has been mainly through hormone replacement therapy (HRT) as well as others such as bisphosphonates and more recently low-dose parathyroid hormone. However, there are side effects reported with this such as tumorigenesis, mood swings, fluid retention and bleeding as well as low compliance of daily injections [44].
\nProbiotics may aid the modulation of the hosts’ inflammatory status by reducing the cytokine secretion levels. The downregulation of proinflammatory cytokines such as IL-6 [45] and TNF-α [46, 47] by probiotics has been reported on several occasions. Studies have shown that some peptides such as p40 and p75 secreted by
The role of the intestinal microbiota has been implicated in influencing bone health. A way by which the intestinal tract aids bone is by the regulation of the absorption of minerals such as calcium, phosphorus, and magnesium. This can also be accomplished by endocrine and gut-derived factors such as incretins and serotonins which may influence bone remodeling. Evidence from using germ-free mice indicated the effect of the intestinal microbiome on bone physiology. These studies observed higher bone mass in germ-free mice as compared to the conventional mice. In addition, a decrease in the number of osteoclasts per bone surface and a reduction in CD4+ T cells and osteoclasts precursors were observed in the bone marrow of the mice [50].
\nThe RANKL/RANK/OPG pathway is one of the mechanisms that influence bone turnover/remodeling. Osteoclast’s formation and activities are controlled by the RANKL/RANK pathway. They are also an essential pathological process of the bone remodeling. Concomitantly, OPG (decoy receptor of RANKL) acts as a bone protector by binding to RANKL and preventing further resorption [42]. Probiotics (beneficial microbes) have been postulated to reduce inflammation [51] and increase OPG expression in bone [52].
\nStudies have shown that various strains of
\n
Probiotics are known to aid mineral absorption for the purpose of bone health maintenance. A study showed that supplementation of growing rats with
Narva et al. demonstrated the effect a bioactive peptide (valylprolyl-proline) and
Studies have also shown that supplementation with
In a study, male senescence-accelerated mice prone to developing osteoporosis with aging were orally administered heat-killed and living (viable)
The growth of bone as an extra-intestinal organ is suppressed by undernutrition in children. The study by Schwarzer et al. indicated that
Furthermore, the effects of probiotics have also been reported in dysbiosis-induced bone loss observed in the periodontal model [67, 68], Type-1 diabetes-induced bone loss [69] and IBD-induced bone loss [70, 71].
\nA human study conducted in Denmark evaluated the combined effects of bioavailable isoflavones and probiotics on bone health and estrogen metabolism using a randomized controlled trial in postmenopausal women. Their findings showed that administration red clover extract (isoflavones) and probiotic attenuated BMD at the lumbar spine and femoral neck, reduced plasma concentrations of C-terminal telopeptide of type I collagen (CTX-1) as well as increased the urinary 2-hydroxyestrone (2-OH) to 16α-hydroxyestrone (16α-OH) ratio (the equol producer status) [72].
\nThe use of probiotics however needs to be administered with caution since although the potential beneficial effect in the treatment of inflammatory and auto-immune gastrointestinal diseases for the modulation of immune response is well recognized, individuals with weaker immune systems may still be at risk of viable bacterial cells; in which case the administration the use of killed/inactivated bacteria might be more beneficial [73].
\nPrebiotics are non-digestible short-chain carbohydrates also known as oligosaccharides (and maybe polysaccharides) which selectively improves the function and activities of specific types of beneficial microbes. The chemical compounds are neither hydrolyzed by the human digestive system nor absorbed in the upper gastrointestinal tract. Prebiotics have been termed ‘colonic foods’ due to the ability of these types of foods to move through the colon serving as a substrate to endogenous bacteria while benefitting the host by providing energy and essential nutrients [74].
\nSome varieties of benefits have been attributed to the consumption of prebiotics. These include the ability of prebiotics to increase the absorption of minerals such as calcium, magnesium, and phosphorus [75, 76, 77, 78] as well as iron [79] as reported quite recently. The absorption of these minerals has consequently been observed to improve bone mineralization and density [80], trabecular structure and increase equol production [81] which is known to reduce bone loss.
\nFOS supplementation has been administered to both Korean [82] and Chinese [83] postmenopausal women to investigate its effect in the prevention of osteoporosis, modulation of bone biomarkers and mineral absorption. Their findings indicate that there is potential for prebiotics to play a pivotal role in the above mentioned. The study by van den Heuvel et al. reported the benefit of intake of both GOS and inulin in increasing calcium absorption in postmenopausal women [84] and oligofructose stimulating calcium absorption in adolescents [85]. Intake of oligofructose-enriched inulin resulted in improved mineral absorption and impacted the bone turnover markers in postmenopausal women [86]. Other studies also looked into the effect of prebiotics in infants as was recorded with GOS, polydextrose [87] and inulin [88]. Some of these studies have also been conducted in animal models as has been shown in a recent review [89].
\nDue to the effect of the change in metabolism from protein fermentation causing the release of ammonia that leads to an increase in pH to more carbohydrate fermentation resulting in the release of acids, a reduction in the intestinal pH is observed. Low intestinal pH tends to increase bowel movement while protecting against pathogens. Diseases such as inflammatory bowel disease (IBD), irritable bowel syndrome (IBS) and Crohn’s diseases are characterized by high pH levels [90]. Prebiotics are therefore able to reduce the symptoms and severity of these diseases. In addition, they are able to restore intestinal bacterial imbalance created by antibiotics, diarrhea, stress and sometimes medication and drugs intake [74].
\nPrebiotics are also known to help relief constipation. Most carbohydrates are able to increase water retention of the intestine and the acids’ production thereby increasing intestinal motility [91]. Furthermore, prebiotics have been used as bioactive functional foods to modulate blood lipid levels [92] and it also been effective in weight loss and metabolic syndrome [93]. The anti-carcinogenic effects of both prebiotics and probiotics have been reported in the inhibition of aberrant crypt foci (ACF) which is a biomarker of colon cancer [94, 95, 96].
\nRecently, prebiotic food and Bidobacterium spp. have been reported to improve bone resorption and reduce serum TRACP-5b levels of Japanese female athletes [97]. Application of the combination of probiotic and prebiotic has been reported to confer a synergistical effect on the host due to the combined benefits of the two. This has been backed with the study by Scholz-Ahrens et al. which showed that probiotics supports the growth of other habitual microbiota strains and prebiotics chain length impacts the composition colonic, caecal, and fecal microflora. The combined administration of oligofructose and
The study of the effect of synbiotics on gut microbiota and bone health profile is now growing rapidly. Probiotic strains have differing genotype and phenotype and may therefore show different metabolic and immunological functions. The mechanisms however still need further investigation to look into the effect of synbiotics on the gut for the regulation of bone metabolism via the process of mineral absorption, the immune, endocrine system. Further studies are needed to elucidate the importance and mechanisms by which prebiotics and probiotics modulates the microbiota-gut-bone axis in order to get the full benefit of the long-term safety and efficacy of consumption of these functional bioactive products.
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With an increasing understanding of clay structure, montmorillonite is realized viable for an enhanced performance in a variety of materials and products in the areas of catalysis, food additive, antibacterial function, polymer, sorbent, etc. Significant development in the use and application of montmorillonite is seen in recent time. This chapter provides an overview of montmorillonite, structure, and properties and particularly discusses its recent utilization in important materials. Montmorillonite is introduced in terms of its natural sources, chemical structure, physical and chemical properties, and functional utilization. The important physical and chemical properties are summarized as particle and layered structure, molecular structure and cation exchange effect, barrier property, and water sorption. This is followed by the important functional utilizations of montmorillonite based on the effects of its chemical structure. The important functional utilization of montmorillonite includes food additive for health and stamina, for antibacterial activity against tooth and gum decay, as sorbent for nonionic, anionic, and cationic dyes, and the use as catalyst in organic synthesis. The environment concerns, to date, do not indicate the adversity for particles used as additive. Studies will be useful which are clearly based on any montmorillonite structure to describe environmental effects.",book:{id:"6561",slug:"current-topics-in-the-utilization-of-clay-in-industrial-and-medical-applications",title:"Current Topics in the Utilization of Clay in Industrial and Medical Applications",fullTitle:"Current Topics in the Utilization of Clay in Industrial and Medical Applications"},signatures:"Faheem Uddin",authors:[{id:"228107",title:"Prof.",name:"Faheem",middleName:null,surname:"Uddin",slug:"faheem-uddin",fullName:"Faheem Uddin"}]},{id:"38850",doi:"10.5772/47790",title:"Clay Minerals from the Perspective of Oil and Gas Exploration",slug:"clay-minerals-from-the-perspective-of-oil-and-gas-exploration",totalDownloads:16067,totalCrossrefCites:17,totalDimensionsCites:44,abstract:null,book:{id:"2328",slug:"clay-minerals-in-nature-their-characterization-modification-and-application",title:"Clay Minerals in Nature",fullTitle:"Clay Minerals in Nature - Their Characterization, Modification and Application"},signatures:"Shu Jiang",authors:[{id:"138867",title:"Dr.",name:"Shu",middleName:null,surname:"Jiang",slug:"shu-jiang",fullName:"Shu Jiang"}]},{id:"38859",doi:"10.5772/51237",title:"Vermiculite: Structural Properties and Examples of the Use",slug:"vermiculite-structural-properties-and-examples-of-the-use",totalDownloads:4763,totalCrossrefCites:8,totalDimensionsCites:42,abstract:null,book:{id:"2328",slug:"clay-minerals-in-nature-their-characterization-modification-and-application",title:"Clay Minerals in Nature",fullTitle:"Clay Minerals in Nature - Their Characterization, Modification and Application"},signatures:"Marta Valášková and Gražyna Simha Martynková",authors:[{id:"128173",title:"Dr.",name:"Marta",middleName:null,surname:"Valaskova",slug:"marta-valaskova",fullName:"Marta Valaskova"}]},{id:"38858",doi:"10.5772/50172",title:"Role of Clay Minerals in Chemical Evolution and the Origins of Life",slug:"role-of-clay-minerals-in-chemical-evolution-and-the-origin-of-life",totalDownloads:4740,totalCrossrefCites:19,totalDimensionsCites:34,abstract:null,book:{id:"2328",slug:"clay-minerals-in-nature-their-characterization-modification-and-application",title:"Clay Minerals in Nature",fullTitle:"Clay Minerals in Nature - Their Characterization, Modification and Application"},signatures:"Hideo Hashizume",authors:[{id:"142318",title:"Dr.",name:"Hideo",middleName:null,surname:"Hashizume",slug:"hideo-hashizume",fullName:"Hideo Hashizume"}]},{id:"38857",doi:"10.5772/50211",title:"Fougerite a Natural Layered Double Hydroxide in Gley Soil: Habitus, Structure, and Some Properties",slug:"fougerite-a-layered-double-hydroxide-in-gley-soil-habitus-structure-and-some-properties",totalDownloads:2824,totalCrossrefCites:7,totalDimensionsCites:20,abstract:null,book:{id:"2328",slug:"clay-minerals-in-nature-their-characterization-modification-and-application",title:"Clay Minerals in Nature",fullTitle:"Clay Minerals in Nature - Their Characterization, Modification and Application"},signatures:"Fabienne Trolard and Guilhem Bourrié",authors:[{id:"149841",title:"Dr.",name:"Fabienne",middleName:null,surname:"Trolard",slug:"fabienne-trolard",fullName:"Fabienne Trolard"},{id:"159630",title:"Dr.",name:"Guilhem",middleName:null,surname:"Bourrié",slug:"guilhem-bourrie",fullName:"Guilhem Bourrié"}]}],mostDownloadedChaptersLast30Days:[{id:"60931",title:"The Importance of Clay in Geotechnical Engineering",slug:"the-importance-of-clay-in-geotechnical-engineering",totalDownloads:5136,totalCrossrefCites:8,totalDimensionsCites:11,abstract:"Clay is a very important material in geotechnical engineering, because it is often observed in geotechnical engineering practice. Generally, this soil type has numerous problems due to its low strength, high compressibility and high level of volumetric changes. Clay needs to be improved before it can be used in road construction, dams, slurry walls, airports and waste landfills. Improved gradation, a reduction in plasticity and swelling potential, as well as an increase in strength and workability, generally improve the stability of clay. Clay is a fine-grained soil, but not all fine-grained soils are clay. Clay minerals are very electrochemically active; thus, they affect soil microstructures. Due to these characteristics, many important soil problems related to clay have been observed in the past, the importance of which is understood. In this chapter, the properties of clay, as well as the use of clay in geotechnical engineering and geotechnical studies on clay, are examined.",book:{id:"6561",slug:"current-topics-in-the-utilization-of-clay-in-industrial-and-medical-applications",title:"Current Topics in the Utilization of Clay in Industrial and Medical Applications",fullTitle:"Current Topics in the Utilization of Clay in Industrial and Medical Applications"},signatures:"Nazile Ural",authors:[{id:"227767",title:"Associate Prof.",name:"Nazile",middleName:null,surname:"Ural",slug:"nazile-ural",fullName:"Nazile Ural"}]},{id:"61845",title:"Montmorillonite: An Introduction to Properties and Utilization",slug:"montmorillonite-an-introduction-to-properties-and-utilization",totalDownloads:5412,totalCrossrefCites:40,totalDimensionsCites:70,abstract:"Clay mineral is an important material available in nature. With an increasing understanding of clay structure, montmorillonite is realized viable for an enhanced performance in a variety of materials and products in the areas of catalysis, food additive, antibacterial function, polymer, sorbent, etc. Significant development in the use and application of montmorillonite is seen in recent time. This chapter provides an overview of montmorillonite, structure, and properties and particularly discusses its recent utilization in important materials. Montmorillonite is introduced in terms of its natural sources, chemical structure, physical and chemical properties, and functional utilization. The important physical and chemical properties are summarized as particle and layered structure, molecular structure and cation exchange effect, barrier property, and water sorption. This is followed by the important functional utilizations of montmorillonite based on the effects of its chemical structure. The important functional utilization of montmorillonite includes food additive for health and stamina, for antibacterial activity against tooth and gum decay, as sorbent for nonionic, anionic, and cationic dyes, and the use as catalyst in organic synthesis. The environment concerns, to date, do not indicate the adversity for particles used as additive. Studies will be useful which are clearly based on any montmorillonite structure to describe environmental effects.",book:{id:"6561",slug:"current-topics-in-the-utilization-of-clay-in-industrial-and-medical-applications",title:"Current Topics in the Utilization of Clay in Industrial and Medical Applications",fullTitle:"Current Topics in the Utilization of Clay in Industrial and Medical Applications"},signatures:"Faheem Uddin",authors:[{id:"228107",title:"Prof.",name:"Faheem",middleName:null,surname:"Uddin",slug:"faheem-uddin",fullName:"Faheem Uddin"}]},{id:"49271",title:"Ceramic Materials Based on Clay Minerals in Cultural Heritage Study",slug:"ceramic-materials-based-on-clay-minerals-in-cultural-heritage-study",totalDownloads:3147,totalCrossrefCites:5,totalDimensionsCites:8,abstract:"The artifacts belonging to the ceramic heritage are mostly based on all clay types used by humans over the ages, because the sources of clays were easily available and people were interested to produce ceramics and pottery. This is the reason why the conservation of cultural heritage is of great concern. Ceramics (Greek κεράμιον Keramion) is a material obtained by shaping and firing clay. In the Romanian history, many ceramic pieces, of great diversity, have been discovered, and most of them are used in traditional households. Ceramic materials based on clay minerals in cultural heritage (ceramic heritage) involve techniques of characterization of raw materials and ceramic objects based on clays, discovered in different archaeological sites, leading to some results about the production technology, provenance, authentication, and historical appartenance on Romanian territory. The chemical composition of ancient ceramics and pigments decorating them, excavated from different Romanian archaeological sites, suggested a chemical composition of ceramic based on clay minerals (kaolinite, illite, and smectite), while the pigments belonging to them contained red pigments (hematite or ocher), manganese oxides (brown pigments), and magnetite or carbon of vegetable origin (black-pigmented layers).",book:{id:"5073",slug:"clays-clay-minerals-and-ceramic-materials-based-on-clay-minerals",title:"Clays, Clay Minerals and Ceramic Materials Based on Clay Minerals",fullTitle:"Clays, Clay Minerals and Ceramic Materials Based on Clay Minerals"},signatures:"Rodica-Mariana Ion, Radu-Claudiu Fierăscu, Sofia Teodorescu, Irina\nFierăscu, Ioana-Raluca Bunghez, Daniela Ţurcanu-Caruţiu and\nMihaela-Lucia Ion",authors:[{id:"137269",title:"Dr.",name:"Radu Claudiu",middleName:null,surname:"Fierascu",slug:"radu-claudiu-fierascu",fullName:"Radu Claudiu Fierascu"},{id:"171504",title:"Prof.",name:"Rodica-Mariana",middleName:null,surname:"Ion",slug:"rodica-mariana-ion",fullName:"Rodica-Mariana Ion"},{id:"176479",title:"Dr.",name:"Sofia",middleName:null,surname:"Teodorescu",slug:"sofia-teodorescu",fullName:"Sofia Teodorescu"},{id:"176480",title:"Dr.",name:"Irina",middleName:null,surname:"Fierascu",slug:"irina-fierascu",fullName:"Irina Fierascu"},{id:"176481",title:"Dr.",name:"Ioana Raluca",middleName:null,surname:"Bunghez",slug:"ioana-raluca-bunghez",fullName:"Ioana Raluca Bunghez"},{id:"176482",title:"Prof.",name:"Daniela",middleName:null,surname:"Turcanu-Carutiu",slug:"daniela-turcanu-carutiu",fullName:"Daniela Turcanu-Carutiu"},{id:"176483",title:"Dr.",name:"Mihaela-Lucia",middleName:null,surname:"Ion",slug:"mihaela-lucia-ion",fullName:"Mihaela-Lucia Ion"}]},{id:"62742",title:"Development of Clay Nanoparticles Toward Bio and Medical Applications",slug:"development-of-clay-nanoparticles-toward-bio-and-medical-applications",totalDownloads:1841,totalCrossrefCites:7,totalDimensionsCites:13,abstract:"Clay nanoparticles are among the most applicable and cost-affordable materials, all of which have a variety of applications in case of medical science. In this chapter, key characteristics of the clay nanoparticles along with their major groups, structure, morphology, and physicochemical properties were evaluated. Thereafter, the applications of clay nanoparticles in the field of nanocomposite, polymeric matrices, and medicine were investigated, while specimen production procedures were also reviewed. The main focus of this chapter is to investigate the applications of clay nanoparticles in bio- and medical science. In fact, organically modified clay nanoparticles (organoclays) are an attractive class of hybrid organic–inorganic nanomaterials with potential applications in case of polymer nanocomposites, rheological properties modification, and drug delivery carrier.",book:{id:"6561",slug:"current-topics-in-the-utilization-of-clay-in-industrial-and-medical-applications",title:"Current Topics in the Utilization of Clay in Industrial and Medical Applications",fullTitle:"Current Topics in the Utilization of Clay in Industrial and Medical Applications"},signatures:"Seyyed Mojtaba Mousavi, Seyyed Alireza Hashemi, Sarvenaz Salahi,\nMojgan Hosseini, Ali Mohammad Amani and Aziz Babapoor",authors:[{id:"208535",title:"M.Sc.",name:"Seyyed Alireza",middleName:null,surname:"Hashemi",slug:"seyyed-alireza-hashemi",fullName:"Seyyed Alireza Hashemi"},{id:"217960",title:"Mr.",name:"Seyyed Mojtaba",middleName:null,surname:"Mousavi",slug:"seyyed-mojtaba-mousavi",fullName:"Seyyed Mojtaba Mousavi"},{id:"217961",title:"Dr.",name:"Ali Mohammad",middleName:null,surname:"Amani",slug:"ali-mohammad-amani",fullName:"Ali Mohammad Amani"}]},{id:"38850",title:"Clay Minerals from the Perspective of Oil and Gas Exploration",slug:"clay-minerals-from-the-perspective-of-oil-and-gas-exploration",totalDownloads:16069,totalCrossrefCites:17,totalDimensionsCites:44,abstract:null,book:{id:"2328",slug:"clay-minerals-in-nature-their-characterization-modification-and-application",title:"Clay Minerals in Nature",fullTitle:"Clay Minerals in Nature - Their Characterization, Modification and Application"},signatures:"Shu Jiang",authors:[{id:"138867",title:"Dr.",name:"Shu",middleName:null,surname:"Jiang",slug:"shu-jiang",fullName:"Shu Jiang"}]}],onlineFirstChaptersFilter:{topicId:"669",limit:6,offset:0},onlineFirstChaptersCollection:[],onlineFirstChaptersTotal:0},preDownload:{success:null,errors:{}},subscriptionForm:{success:null,errors:{}},aboutIntechopen:{},privacyPolicy:{},peerReviewing:{},howOpenAccessPublishingWithIntechopenWorks:{},sponsorshipBooks:{sponsorshipBooks:[],offset:8,limit:8,total:0},allSeries:{pteSeriesList:[{id:"14",title:"Artificial Intelligence",numberOfPublishedBooks:8,numberOfPublishedChapters:87,numberOfOpenTopics:6,numberOfUpcomingTopics:0,issn:"2633-1403",doi:"10.5772/intechopen.79920",isOpenForSubmission:!0},{id:"7",title:"Biomedical Engineering",numberOfPublishedBooks:12,numberOfPublishedChapters:98,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2631-5343",doi:"10.5772/intechopen.71985",isOpenForSubmission:!0}],lsSeriesList:[{id:"11",title:"Biochemistry",numberOfPublishedBooks:27,numberOfPublishedChapters:286,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2632-0983",doi:"10.5772/intechopen.72877",isOpenForSubmission:!0},{id:"25",title:"Environmental Sciences",numberOfPublishedBooks:1,numberOfPublishedChapters:9,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2754-6713",doi:"10.5772/intechopen.100362",isOpenForSubmission:!0},{id:"10",title:"Physiology",numberOfPublishedBooks:11,numberOfPublishedChapters:139,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2631-8261",doi:"10.5772/intechopen.72796",isOpenForSubmission:!0}],hsSeriesList:[{id:"3",title:"Dentistry",numberOfPublishedBooks:8,numberOfPublishedChapters:129,numberOfOpenTopics:0,numberOfUpcomingTopics:2,issn:"2631-6218",doi:"10.5772/intechopen.71199",isOpenForSubmission:!1},{id:"6",title:"Infectious Diseases",numberOfPublishedBooks:13,numberOfPublishedChapters:106,numberOfOpenTopics:3,numberOfUpcomingTopics:1,issn:"2631-6188",doi:"10.5772/intechopen.71852",isOpenForSubmission:!0},{id:"13",title:"Veterinary Medicine and Science",numberOfPublishedBooks:9,numberOfPublishedChapters:101,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2632-0517",doi:"10.5772/intechopen.73681",isOpenForSubmission:!0}],sshSeriesList:[{id:"22",title:"Business, Management and Economics",numberOfPublishedBooks:1,numberOfPublishedChapters:11,numberOfOpenTopics:2,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100359",isOpenForSubmission:!0},{id:"23",title:"Education and Human Development",numberOfPublishedBooks:0,numberOfPublishedChapters:0,numberOfOpenTopics:2,numberOfUpcomingTopics:0,issn:null,doi:"10.5772/intechopen.100360",isOpenForSubmission:!1},{id:"24",title:"Sustainable Development",numberOfPublishedBooks:0,numberOfPublishedChapters:9,numberOfOpenTopics:4,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100361",isOpenForSubmission:!0}],testimonialsList:[{id:"6",text:"It is great to work with the IntechOpen to produce a worthwhile collection of research that also becomes a great educational resource and guide for future research endeavors.",author:{id:"259298",name:"Edward",surname:"Narayan",institutionString:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259298/images/system/259298.jpeg",slug:"edward-narayan",institution:{id:"3",name:"University of Queensland",country:{id:null,name:"Australia"}}}},{id:"13",text:"The collaboration with and support of the technical staff of IntechOpen is fantastic. The whole process of submitting an article and editing of the submitted article goes extremely smooth and fast, the number of reads and downloads of chapters is high, and the contributions are also frequently cited.",author:{id:"55578",name:"Antonio",surname:"Jurado-Navas",institutionString:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRisIQAS/Profile_Picture_1626166543950",slug:"antonio-jurado-navas",institution:{id:"720",name:"University of Malaga",country:{id:null,name:"Spain"}}}}]},series:{item:{id:"10",title:"Physiology",doi:"10.5772/intechopen.72796",issn:"2631-8261",scope:"Modern physiology requires a comprehensive understanding of the integration of tissues and organs throughout the mammalian body, including the cooperation between structure and function at the cellular and molecular levels governed by gene and protein expression. While a daunting task, learning is facilitated by identifying common and effective signaling pathways mediated by a variety of factors employed by nature to preserve and sustain homeostatic life. \r\nAs a leading example, the cellular interaction between intracellular concentration of Ca+2 increases, and changes in plasma membrane potential is integral for coordinating blood flow, governing the exocytosis of neurotransmitters, and modulating gene expression and cell effector secretory functions. Furthermore, in this manner, understanding the systemic interaction between the cardiovascular and nervous systems has become more important than ever as human populations' life prolongation, aging and mechanisms of cellular oxidative signaling are utilised for sustaining life. \r\nAltogether, physiological research enables our identification of distinct and precise points of transition from health to the development of multimorbidity throughout the inevitable aging disorders (e.g., diabetes, hypertension, chronic kidney disease, heart failure, peptic ulcer, inflammatory bowel disease, age-related macular degeneration, cancer). With consideration of all organ systems (e.g., brain, heart, lung, gut, skeletal and smooth muscle, liver, pancreas, kidney, eye) and the interactions thereof, this Physiology Series will address the goals of resolving (1) Aging physiology and chronic disease progression (2) Examination of key cellular pathways as they relate to calcium, oxidative stress, and electrical signaling, and (3) how changes in plasma membrane produced by lipid peroxidation products can affect aging physiology, covering new research in the area of cell, human, plant and animal physiology.",coverUrl:"https://cdn.intechopen.com/series/covers/10.jpg",latestPublicationDate:"May 14th, 2022",hasOnlineFirst:!0,numberOfPublishedBooks:11,editor:{id:"35854",title:"Prof.",name:"Tomasz",middleName:null,surname:"Brzozowski",slug:"tomasz-brzozowski",fullName:"Tomasz Brzozowski",profilePictureURL:"https://mts.intechopen.com/storage/users/35854/images/system/35854.jpg",biography:"Prof. Dr. Thomas Brzozowski works as a professor of Human Physiology and is currently Chairman at the Department of Physiology and is V-Dean of the Medical Faculty at Jagiellonian University Medical College, Cracow, Poland. His primary area of interest is physiology and pathophysiology of the gastrointestinal (GI) tract, with the major focus on the mechanism of GI mucosal defense, protection, and ulcer healing. He was a postdoctoral NIH fellow at the University of California and the Gastroenterology VA Medical Center, Irvine, Long Beach, CA, USA, and at the Gastroenterology Clinics Erlangen-Nuremberg and Munster in Germany. He has published 290 original articles in some of the most prestigious scientific journals and seven book chapters on the pathophysiology of the GI tract, gastroprotection, ulcer healing, drug therapy of peptic ulcers, hormonal regulation of the gut, and inflammatory bowel disease.",institutionString:null,institution:{name:"Jagiellonian University",institutionURL:null,country:{name:"Poland"}}},editorTwo:null,editorThree:null},subseries:{paginationCount:7,paginationItems:[{id:"10",title:"Animal Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/10.jpg",editor:{id:"202192",title:"Dr.",name:"Catrin",middleName:null,surname:"Rutland",slug:"catrin-rutland",fullName:"Catrin Rutland",profilePictureURL:"https://mts.intechopen.com/storage/users/202192/images/system/202192.png",biography:"Catrin Rutland is an Associate Professor of Anatomy and Developmental Genetics at the University of Nottingham, UK. She obtained a BSc from the University of Derby, England, a master’s degree from Technische Universität München, Germany, and a Ph.D. from the University of Nottingham. She undertook a post-doctoral research fellowship in the School of Medicine before accepting tenure in Veterinary Medicine and Science. Dr. Rutland also obtained an MMedSci (Medical Education) and a Postgraduate Certificate in Higher Education (PGCHE). She is the author of more than sixty peer-reviewed journal articles, twelve books/book chapters, and more than 100 research abstracts in cardiovascular biology and oncology. She is a board member of the European Association of Veterinary Anatomists, Fellow of the Anatomical Society, and Senior Fellow of the Higher Education Academy. Dr. Rutland has also written popular science books for the public. https://orcid.org/0000-0002-2009-4898. www.nottingham.ac.uk/vet/people/catrin.rutland",institutionString:null,institution:{name:"University of Nottingham",institutionURL:null,country:{name:"United Kingdom"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"306970",title:"Mr.",name:"Amin",middleName:null,surname:"Tamadon",slug:"amin-tamadon",fullName:"Amin Tamadon",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002oHR5wQAG/Profile_Picture_1623910304139",institutionString:null,institution:{name:"Bushehr University of Medical Sciences",institutionURL:null,country:{name:"Iran"}}},{id:"251314",title:"Dr.",name:"Juan Carlos",middleName:null,surname:"Gardón",slug:"juan-carlos-gardon",fullName:"Juan Carlos Gardón",profilePictureURL:"https://mts.intechopen.com/storage/users/251314/images/system/251314.jpeg",institutionString:"Catholic University of Valencia San Vicente Mártir, Spain",institution:null},{id:"245306",title:"Dr.",name:"María Luz",middleName:null,surname:"Garcia Pardo",slug:"maria-luz-garcia-pardo",fullName:"María Luz Garcia Pardo",profilePictureURL:"https://mts.intechopen.com/storage/users/245306/images/system/245306.png",institutionString:null,institution:{name:"Miguel Hernandez University",institutionURL:null,country:{name:"Spain"}}},{id:"283315",title:"Prof.",name:"Samir",middleName:null,surname:"El-Gendy",slug:"samir-el-gendy",fullName:"Samir El-Gendy",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRduYQAS/Profile_Picture_1606215849748",institutionString:null,institution:{name:"Alexandria University",institutionURL:null,country:{name:"Egypt"}}}]},{id:"11",title:"Cell Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/11.jpg",editor:{id:"133493",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",profilePictureURL:"https://mts.intechopen.com/storage/users/133493/images/3091_n.jpg",biography:"Prof. Dr. Angel Catalá \r\nShort Biography Angel Catalá was born in Rodeo (San Juan, Argentina). He studied \r\nchemistry at the Universidad Nacional de La Plata, Argentina, where received aPh.D. degree in chemistry (Biological Branch) in 1965. From\r\n1964 to 1974, he worked as Assistant in Biochemistry at the School of MedicineUniversidad Nacional de La Plata, Argentina. From 1974 to 1976, he was a Fellowof the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor oBiochemistry at the Universidad Nacional de La Plata, Argentina. He is Member ofthe National Research Council (CONICET), Argentina, and Argentine Society foBiochemistry and Molecular Biology (SAIB). His laboratory has been interested for manyears in the lipid peroxidation of biological membranes from various tissues and different species. Professor Catalá has directed twelve doctoral theses, publishedover 100 papers in peer reviewed journals, several chapters in books andtwelve edited books. Angel Catalá received awards at the 40th InternationaConference Biochemistry of Lipids 1999: Dijon (France). W inner of the Bimbo PanAmerican Nutrition, Food Science and Technology Award 2006 and 2012, South AmericaHuman Nutrition, Professional Category. 2006 award in pharmacology, Bernardo\r\nHoussay, in recognition of his meritorious works of research. Angel Catalá belongto the Editorial Board of Journal of lipids, International Review of Biophysical ChemistryFrontiers in Membrane Physiology and Biophysics, World Journal oExperimental Medicine and Biochemistry Research International, W orld Journal oBiological Chemistry, Oxidative Medicine and Cellular Longevity, Diabetes and thePancreas, International Journal of Chronic Diseases & Therapy, International Journal oNutrition, Co-Editor of The Open Biology Journal.",institutionString:null,institution:{name:"National University of La Plata",institutionURL:null,country:{name:"Argentina"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"186048",title:"Prof.",name:"Ines",middleName:null,surname:"Drenjančević",slug:"ines-drenjancevic",fullName:"Ines Drenjančević",profilePictureURL:"https://mts.intechopen.com/storage/users/186048/images/5818_n.jpg",institutionString:null,institution:{name:"University of Osijek",institutionURL:null,country:{name:"Croatia"}}},{id:"187859",title:"Prof.",name:"Kusal",middleName:"K.",surname:"Das",slug:"kusal-das",fullName:"Kusal Das",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSBDeQAO/Profile_Picture_1623411145568",institutionString:"BLDE (Deemed to be University), India",institution:null},{id:"79615",title:"Dr.",name:"Robson",middleName:null,surname:"Faria",slug:"robson-faria",fullName:"Robson Faria",profilePictureURL:"https://mts.intechopen.com/storage/users/79615/images/system/79615.png",institutionString:null,institution:{name:"Oswaldo Cruz Foundation",institutionURL:null,country:{name:"Brazil"}}},{id:"84459",title:"Prof.",name:"Valerie",middleName:null,surname:"Chappe",slug:"valerie-chappe",fullName:"Valerie Chappe",profilePictureURL:"https://mts.intechopen.com/storage/users/84459/images/system/84459.jpg",institutionString:null,institution:{name:"Dalhousie University",institutionURL:null,country:{name:"Canada"}}}]},{id:"12",title:"Human Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/12.jpg",editor:{id:"195829",title:"Prof.",name:"Kunihiro",middleName:null,surname:"Sakuma",slug:"kunihiro-sakuma",fullName:"Kunihiro Sakuma",profilePictureURL:"https://mts.intechopen.com/storage/users/195829/images/system/195829.jpg",biography:"Professor Kunihiro Sakuma, Ph.D., currently works in the Institute for Liberal Arts at the Tokyo Institute of Technology. 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His research interest focuses on computational chemistry and molecular modeling of diverse systems of pharmacological, food, and alternative energy interests by resorting to DFT and Conceptual DFT. He has authored a coauthored more than 255 peer-reviewed papers, 32 book chapters, and 2 edited books. He has delivered speeches at many international and domestic conferences. He serves as a reviewer for more than eighty international journals, books, and research proposals as well as an editor for special issues of renowned scientific journals.",institutionString:"Centro de Investigación en Materiales Avanzados",institution:{name:"Centro de Investigación en Materiales Avanzados",country:{name:"Mexico"}}},{id:"76477",title:"Prof.",name:"Mirza",middleName:null,surname:"Hasanuzzaman",slug:"mirza-hasanuzzaman",fullName:"Mirza Hasanuzzaman",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/76477/images/system/76477.png",biography:"Dr. Mirza Hasanuzzaman is a Professor of Agronomy at Sher-e-Bangla Agricultural University, Bangladesh. He received his Ph.D. in Plant Stress Physiology and Antioxidant Metabolism from Ehime University, Japan, with a scholarship from the Japanese Government (MEXT). Later, he completed his postdoctoral research at the Center of Molecular Biosciences, University of the Ryukyus, Japan, as a recipient of the Japan Society for the Promotion of Science (JSPS) postdoctoral fellowship. He was also the recipient of the Australian Government Endeavour Research Fellowship for postdoctoral research as an adjunct senior researcher at the University of Tasmania, Australia. Dr. Hasanuzzaman’s current work is focused on the physiological and molecular mechanisms of environmental stress tolerance. Dr. Hasanuzzaman has published more than 150 articles in peer-reviewed journals. He has edited ten books and written more than forty book chapters on important aspects of plant physiology, plant stress tolerance, and crop production. According to Scopus, Dr. Hasanuzzaman’s publications have received more than 10,500 citations with an h-index of 53. He has been named a Highly Cited Researcher by Clarivate. He is an editor and reviewer for more than fifty peer-reviewed international journals and was a recipient of the “Publons Peer Review Award” in 2017, 2018, and 2019. He has been honored by different authorities for his outstanding performance in various fields like research and education, and he has received the World Academy of Science Young Scientist Award (2014) and the University Grants Commission (UGC) Award 2018. He is a fellow of the Bangladesh Academy of Sciences (BAS) and the Royal Society of Biology.",institutionString:"Sher-e-Bangla Agricultural University",institution:{name:"Sher-e-Bangla Agricultural University",country:{name:"Bangladesh"}}},{id:"187859",title:"Prof.",name:"Kusal",middleName:"K.",surname:"Das",slug:"kusal-das",fullName:"Kusal Das",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSBDeQAO/Profile_Picture_1623411145568",biography:"Kusal K. Das is a Distinguished Chair Professor of Physiology, Shri B. M. Patil Medical College and Director, Centre for Advanced Medical Research (CAMR), BLDE (Deemed to be University), Vijayapur, Karnataka, India. Dr. Das did his M.S. and Ph.D. in Human Physiology from the University of Calcutta, Kolkata. His area of research is focused on understanding of molecular mechanisms of heavy metal activated low oxygen sensing pathways in vascular pathophysiology. He has invented a new method of estimation of serum vitamin E. His expertise in critical experimental protocols on vascular functions in experimental animals was well documented by his quality of publications. He was a Visiting Professor of Medicine at University of Leeds, United Kingdom (2014-2016) and Tulane University, New Orleans, USA (2017). For his immense contribution in medical research Ministry of Science and Technology, Government of India conferred him 'G.P. Chatterjee Memorial Research Prize-2019” and he is also the recipient of 'Dr.Raja Ramanna State Scientist Award 2015” by Government of Karnataka. He is a Fellow of the Royal Society of Biology (FRSB), London and Honorary Fellow of Karnataka Science and Technology Academy, Department of Science and Technology, Government of Karnataka.",institutionString:"BLDE (Deemed to be University), India",institution:null},{id:"243660",title:"Dr.",name:"Mallanagouda Shivanagouda",middleName:null,surname:"Biradar",slug:"mallanagouda-shivanagouda-biradar",fullName:"Mallanagouda Shivanagouda Biradar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/243660/images/system/243660.jpeg",biography:"M. S. Biradar is Vice Chancellor and Professor of Medicine of\nBLDE (Deemed to be University), Vijayapura, Karnataka, India.\nHe obtained his MD with a gold medal in General Medicine and\nhas devoted himself to medical teaching, research, and administrations. He has also immensely contributed to medical research\non vascular medicine, which is reflected by his numerous publications including books and book chapters. Professor Biradar was\nalso Visiting Professor at Tulane University School of Medicine, New Orleans, USA.",institutionString:"BLDE (Deemed to be University)",institution:{name:"BLDE University",country:{name:"India"}}},{id:"289796",title:"Dr.",name:"Swastika",middleName:null,surname:"Das",slug:"swastika-das",fullName:"Swastika Das",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/289796/images/system/289796.jpeg",biography:"Swastika N. Das is Professor of Chemistry at the V. P. Dr. P. G.\nHalakatti College of Engineering and Technology, BLDE (Deemed\nto be University), Vijayapura, Karnataka, India. She obtained an\nMSc, MPhil, and PhD in Chemistry from Sambalpur University,\nOdisha, India. Her areas of research interest are medicinal chemistry, chemical kinetics, and free radical chemistry. She is a member\nof the investigators who invented a new modified method of estimation of serum vitamin E. She has authored numerous publications including book\nchapters and is a mentor of doctoral curriculum at her university.",institutionString:"BLDEA’s V.P.Dr.P.G.Halakatti College of Engineering & Technology",institution:{name:"BLDE University",country:{name:"India"}}},{id:"248459",title:"Dr.",name:"Akikazu",middleName:null,surname:"Takada",slug:"akikazu-takada",fullName:"Akikazu Takada",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/248459/images/system/248459.png",biography:"Akikazu Takada was born in Japan, 1935. After graduation from\nKeio University School of Medicine and finishing his post-graduate studies, he worked at Roswell Park Memorial Institute NY,\nUSA. He then took a professorship at Hamamatsu University\nSchool of Medicine. In thrombosis studies, he found the SK\npotentiator that enhances plasminogen activation by streptokinase. He is very much interested in simultaneous measurements\nof fatty acids, amino acids, and tryptophan degradation products. By using fatty\nacid analyses, he indicated that plasma levels of trans-fatty acids of old men were\nfar higher in the US than Japanese men. . He also showed that eicosapentaenoic acid\n(EPA) and docosahexaenoic acid (DHA) levels are higher, and arachidonic acid\nlevels are lower in Japanese than US people. By using simultaneous LC/MS analyses\nof plasma levels of tryptophan metabolites, he recently found that plasma levels of\nserotonin, kynurenine, or 5-HIAA were higher in patients of mono- and bipolar\ndepression, which are significantly different from observations reported before. In\nview of recent reports that plasma tryptophan metabolites are mainly produced by\nmicrobiota. He is now working on the relationships between microbiota and depression or autism.",institutionString:"Hamamatsu University School of Medicine",institution:{name:"Hamamatsu University School of Medicine",country:{name:"Japan"}}},{id:"137240",title:"Prof.",name:"Mohammed",middleName:null,surname:"Khalid",slug:"mohammed-khalid",fullName:"Mohammed Khalid",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/137240/images/system/137240.png",biography:"Mohammed Khalid received his B.S. degree in chemistry in 2000 and Ph.D. degree in physical chemistry in 2007 from the University of Khartoum, Sudan. He moved to School of Chemistry, Faculty of Science, University of Sydney, Australia in 2009 and joined Dr. Ron Clarke as a postdoctoral fellow where he worked on the interaction of ATP with the phosphoenzyme of the Na+/K+-ATPase and dual mechanisms of allosteric acceleration of the Na+/K+-ATPase by ATP; then he went back to Department of Chemistry, University of Khartoum as an assistant professor, and in 2014 he was promoted as an associate professor. In 2011, he joined the staff of Department of Chemistry at Taif University, Saudi Arabia, where he is currently an assistant professor. His research interests include the following: P-Type ATPase enzyme kinetics and mechanisms, kinetics and mechanisms of redox reactions, autocatalytic reactions, computational enzyme kinetics, allosteric acceleration of P-type ATPases by ATP, exploring of allosteric sites of ATPases, and interaction of ATP with ATPases located in cell membranes.",institutionString:"Taif University",institution:{name:"Taif University",country:{name:"Saudi Arabia"}}},{id:"63810",title:"Prof.",name:"Jorge",middleName:null,surname:"Morales-Montor",slug:"jorge-morales-montor",fullName:"Jorge Morales-Montor",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/63810/images/system/63810.png",biography:"Dr. Jorge Morales-Montor was recognized with the Lola and Igo Flisser PUIS Award for best graduate thesis at the national level in the field of parasitology. He received a fellowship from the Fogarty Foundation to perform postdoctoral research stay at the University of Georgia. He has 153 journal articles to his credit. He has also edited several books and published more than fifty-five book chapters. He is a member of the Mexican Academy of Sciences, Latin American Academy of Sciences, and the National Academy of Medicine. He has received more than thirty-five awards and has supervised numerous bachelor’s, master’s, and Ph.D. students. Dr. Morales-Montor is the past president of the Mexican Society of Parasitology.",institutionString:"National Autonomous University of Mexico",institution:{name:"National Autonomous University of Mexico",country:{name:"Mexico"}}},{id:"217215",title:"Dr.",name:"Palash",middleName:null,surname:"Mandal",slug:"palash-mandal",fullName:"Palash Mandal",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217215/images/system/217215.jpeg",biography:null,institutionString:"Charusat University",institution:null},{id:"49739",title:"Dr.",name:"Leszek",middleName:null,surname:"Szablewski",slug:"leszek-szablewski",fullName:"Leszek Szablewski",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49739/images/system/49739.jpg",biography:"Leszek Szablewski is a professor of medical sciences. He received his M.S. in the Faculty of Biology from the University of Warsaw and his PhD degree from the Institute of Experimental Biology Polish Academy of Sciences. He habilitated in the Medical University of Warsaw, and he obtained his degree of Professor from the President of Poland. Professor Szablewski is the Head of Chair and Department of General Biology and Parasitology, Medical University of Warsaw. Professor Szablewski has published over 80 peer-reviewed papers in journals such as Journal of Alzheimer’s Disease, Biochim. Biophys. Acta Reviews of Cancer, Biol. Chem., J. Biomed. Sci., and Diabetes/Metabol. Res. Rev, Endocrine. He is the author of two books and four book chapters. He has edited four books, written 15 scripts for students, is the ad hoc reviewer of over 30 peer-reviewed journals, and editorial member of peer-reviewed journals. Prof. Szablewski’s research focuses on cell physiology, genetics, and pathophysiology. He works on the damage caused by lack of glucose homeostasis and changes in the expression and/or function of glucose transporters due to various diseases. He has given lectures, seminars, and exercises for students at the Medical University.",institutionString:"Medical University of Warsaw",institution:{name:"Medical University of Warsaw",country:{name:"Poland"}}},{id:"173123",title:"Dr.",name:"Maitham",middleName:null,surname:"Khajah",slug:"maitham-khajah",fullName:"Maitham Khajah",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/173123/images/system/173123.jpeg",biography:"Dr. Maitham A. Khajah received his degree in Pharmacy from Faculty of Pharmacy, Kuwait University, in 2003 and obtained his PhD degree in December 2009 from the University of Calgary, Canada (Gastrointestinal Science and Immunology). Since January 2010 he has been assistant professor in Kuwait University, Faculty of Pharmacy, Department of Pharmacology and Therapeutics. His research interest are molecular targets for the treatment of inflammatory bowel disease (IBD) and the mechanisms responsible for immune cell chemotaxis. He cosupervised many students for the MSc Molecular Biology Program, College of Graduate Studies, Kuwait University. Ever since joining Kuwait University in 2010, he got various grants as PI and Co-I. He was awarded the Best Young Researcher Award by Kuwait University, Research Sector, for the Year 2013–2014. He was a member in the organizing committee for three conferences organized by Kuwait University, Faculty of Pharmacy, as cochair and a member in the scientific committee (the 3rd, 4th, and 5th Kuwait International Pharmacy Conference).",institutionString:"Kuwait University",institution:{name:"Kuwait University",country:{name:"Kuwait"}}},{id:"195136",title:"Dr.",name:"Aya",middleName:null,surname:"Adel",slug:"aya-adel",fullName:"Aya Adel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/195136/images/system/195136.jpg",biography:"Dr. Adel works as an Assistant Lecturer in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. Dr. Adel is especially interested in joint attention and its impairment in autism spectrum disorder",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"94911",title:"Dr.",name:"Boulenouar",middleName:null,surname:"Mesraoua",slug:"boulenouar-mesraoua",fullName:"Boulenouar Mesraoua",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94911/images/system/94911.png",biography:"Dr Boulenouar Mesraoua is the Associate Professor of Clinical Neurology at Weill Cornell Medical College-Qatar and a Consultant Neurologist at Hamad Medical Corporation at the Neuroscience Department; He graduated as a Medical Doctor from the University of Oran, Algeria; he then moved to Belgium, the City of Liege, for a Residency in Internal Medicine and Neurology at Liege University; after getting the Belgian Board of Neurology (with high marks), he went to the National Hospital for Nervous Diseases, Queen Square, London, United Kingdom for a fellowship in Clinical Neurophysiology, under Pr Willison ; Dr Mesraoua had also further training in Epilepsy and Continuous EEG Monitoring for two years (from 2001-2003) in the Neurophysiology department of Zurich University, Switzerland, under late Pr Hans Gregor Wieser ,an internationally known epileptologist expert. \n\nDr B. Mesraoua is the Director of the Neurology Fellowship Program at the Neurology Section and an active member of the newly created Comprehensive Epilepsy Program at Hamad General Hospital, Doha, Qatar; he is also Assistant Director of the Residency Program at the Qatar Medical School. \nDr B. Mesraoua's main interests are Epilepsy, Multiple Sclerosis, and Clinical Neurology; He is the Chairman and the Organizer of the well known Qatar Epilepsy Symposium, he is running yearly for the past 14 years and which is considered a landmark in the Gulf region; He has also started last year , together with other epileptologists from Qatar, the region and elsewhere, a yearly International Epilepsy School Course, which was attended by many neurologists from the Area.\n\nInternationally, Dr Mesraoua is an active and elected member of the Commission on Eastern Mediterranean Region (EMR ) , a regional branch of the International League Against Epilepsy (ILAE), where he represents the Middle East and North Africa(MENA ) and where he holds the position of chief of the Epilepsy Epidemiology Section; Dr Mesraoua is a member of the American Academy of Neurology, the Europeen Academy of Neurology and the American Epilepsy Society.\n\nDr Mesraoua's main objectives are to encourage frequent gathering of the epileptologists/neurologists from the MENA region and the rest of the world, promote Epilepsy Teaching in the MENA Region, and encourage multicenter studies involving neurologists and epileptologists in the MENA region, particularly epilepsy epidemiological studies. \n\nDr. Mesraoua is the recipient of two research Grants, as the Lead Principal Investigator (750.000 USD and 250.000 USD) from the Qatar National Research Fund (QNRF) and the Hamad Hospital Internal Research Grant (IRGC), on the following topics : “Continuous EEG Monitoring in the ICU “ and on “Alpha-lactoalbumin , proof of concept in the treatment of epilepsy” .Dr Mesraoua is a reviewer for the journal \"seizures\" (Europeen Epilepsy Journal ) as well as dove journals ; Dr Mesraoua is the author and co-author of many peer reviewed publications and four book chapters in the field of Epilepsy and Clinical Neurology",institutionString:"Weill Cornell Medical College in Qatar",institution:{name:"Weill Cornell Medical College in Qatar",country:{name:"Qatar"}}},{id:"282429",title:"Prof.",name:"Covanis",middleName:null,surname:"Athanasios",slug:"covanis-athanasios",fullName:"Covanis Athanasios",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/282429/images/system/282429.jpg",biography:null,institutionString:"Neurology-Neurophysiology Department of the Children Hospital Agia Sophia",institution:null},{id:"190980",title:"Prof.",name:"Marwa",middleName:null,surname:"Mahmoud Saleh",slug:"marwa-mahmoud-saleh",fullName:"Marwa Mahmoud Saleh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/190980/images/system/190980.jpg",biography:"Professor Marwa Mahmoud Saleh is a doctor of medicine and currently works in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. She got her doctoral degree in 1991 and her doctoral thesis was accomplished in the University of Iowa, United States. Her publications covered a multitude of topics as videokymography, cochlear implants, stuttering, and dysphagia. She has lectured Egyptian phonology for many years. Her recent research interest is joint attention in autism.",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"259190",title:"Dr.",name:"Syed Ali Raza",middleName:null,surname:"Naqvi",slug:"syed-ali-raza-naqvi",fullName:"Syed Ali Raza Naqvi",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259190/images/system/259190.png",biography:"Dr. Naqvi is a radioanalytical chemist and is working as an associate professor of analytical chemistry in the Department of Chemistry, Government College University, Faisalabad, Pakistan. Advance separation techniques, nuclear analytical techniques and radiopharmaceutical analysis are the main courses that he is teaching to graduate and post-graduate students. In the research area, he is focusing on the development of organic- and biomolecule-based radiopharmaceuticals for diagnosis and therapy of infectious and cancerous diseases. Under the supervision of Dr. Naqvi, three students have completed their Ph.D. degrees and 41 students have completed their MS degrees. He has completed three research projects and is currently working on 2 projects entitled “Radiolabeling of fluoroquinolone derivatives for the diagnosis of deep-seated bacterial infections” and “Radiolabeled minigastrin peptides for diagnosis and therapy of NETs”. He has published about 100 research articles in international reputed journals and 7 book chapters. Pakistan Institute of Nuclear Science & Technology (PINSTECH) Islamabad, Punjab Institute of Nuclear Medicine (PINM), Faisalabad and Institute of Nuclear Medicine and Radiology (INOR) Abbottabad are the main collaborating institutes.",institutionString:"Government College University",institution:{name:"Government College University, Faisalabad",country:{name:"Pakistan"}}},{id:"58390",title:"Dr.",name:"Gyula",middleName:null,surname:"Mozsik",slug:"gyula-mozsik",fullName:"Gyula Mozsik",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/58390/images/system/58390.png",biography:"Gyula Mózsik MD, Ph.D., ScD (med), is an emeritus professor of Medicine at the First Department of Medicine, Univesity of Pécs, Hungary. He was head of this department from 1993 to 2003. His specializations are medicine, gastroenterology, clinical pharmacology, clinical nutrition, and dietetics. His research fields are biochemical pharmacological examinations in the human gastrointestinal (GI) mucosa, mechanisms of retinoids, drugs, capsaicin-sensitive afferent nerves, and innovative pharmacological, pharmaceutical, and nutritional (dietary) research in humans. He has published about 360 peer-reviewed papers, 197 book chapters, 692 abstracts, 19 monographs, and has edited 37 books. He has given about 1120 regular and review lectures. He has organized thirty-eight national and international congresses and symposia. He is the founder of the International Conference on Ulcer Research (ICUR); International Union of Pharmacology, Gastrointestinal Section (IUPHAR-GI); Brain-Gut Society symposiums, and gastrointestinal cytoprotective symposiums. He received the Andre Robert Award from IUPHAR-GI in 2014. Fifteen of his students have been appointed as full professors in Egypt, Cuba, and Hungary.",institutionString:"University of Pécs",institution:{name:"University of Pecs",country:{name:"Hungary"}}},{id:"277367",title:"M.Sc.",name:"Daniel",middleName:"Martin",surname:"Márquez López",slug:"daniel-marquez-lopez",fullName:"Daniel Márquez López",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/277367/images/7909_n.jpg",biography:"Msc Daniel Martin Márquez López has a bachelor degree in Industrial Chemical Engineering, a Master of science degree in the same área and he is a PhD candidate for the Instituto Politécnico Nacional. His Works are realted to the Green chemistry field, biolubricants, biodiesel, transesterification reactions for biodiesel production and the manipulation of oils for therapeutic purposes.",institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"196544",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/196544/images/system/196544.jpg",biography:"Angel Catalá studied chemistry at Universidad Nacional de La Plata, Argentina, where he received a Ph.D. in Chemistry (Biological Branch) in 1965. From 1964 to 1974, he worked as an Assistant in Biochemistry at the School of Medicine at the same university. From 1974 to 1976, he was a fellow of the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor of Biochemistry at the Universidad Nacional de La Plata. He is a member of the National Research Council (CONICET), Argentina, and the Argentine Society for Biochemistry and Molecular Biology (SAIB). His laboratory has been interested for many years in the lipid peroxidation of biological membranes from various tissues and different species. Dr. Catalá has directed twelve doctoral theses, published more than 100 papers in peer-reviewed journals, several chapters in books, and edited twelve books. He received awards at the 40th International Conference Biochemistry of Lipids 1999 in Dijon, France. He is the winner of the Bimbo Pan-American Nutrition, Food Science and Technology Award 2006 and 2012, South America, Human Nutrition, Professional Category. In 2006, he won the Bernardo Houssay award in pharmacology, in recognition of his meritorious works of research. Dr. Catalá belongs to the editorial board of several journals including Journal of Lipids; International Review of Biophysical Chemistry; Frontiers in Membrane Physiology and Biophysics; World Journal of Experimental Medicine and Biochemistry Research International; World Journal of Biological Chemistry, Diabetes, and the Pancreas; International Journal of Chronic Diseases & Therapy; and International Journal of Nutrition. He is the co-editor of The Open Biology Journal and associate editor for Oxidative Medicine and Cellular Longevity.",institutionString:"Universidad Nacional de La Plata",institution:{name:"National University of La Plata",country:{name:"Argentina"}}},{id:"186585",title:"Dr.",name:"Francisco Javier",middleName:null,surname:"Martin-Romero",slug:"francisco-javier-martin-romero",fullName:"Francisco Javier Martin-Romero",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSB3HQAW/Profile_Picture_1631258137641",biography:"Francisco Javier Martín-Romero (Javier) is a Professor of Biochemistry and Molecular Biology at the University of Extremadura, Spain. He is also a group leader at the Biomarkers Institute of Molecular Pathology. Javier received his Ph.D. in 1998 in Biochemistry and Biophysics. At the National Cancer Institute (National Institute of Health, Bethesda, MD) he worked as a research associate on the molecular biology of selenium and its role in health and disease. After postdoctoral collaborations with Carlos Gutierrez-Merino (University of Extremadura, Spain) and Dario Alessi (University of Dundee, UK), he established his own laboratory in 2008. The interest of Javier's lab is the study of cell signaling with a special focus on Ca2+ signaling, and how Ca2+ transport modulates the cytoskeleton, migration, differentiation, cell death, etc. He is especially interested in the study of Ca2+ channels, and the role of STIM1 in the initiation of pathological events.",institutionString:null,institution:{name:"University of Extremadura",country:{name:"Spain"}}},{id:"217323",title:"Prof.",name:"Guang-Jer",middleName:null,surname:"Wu",slug:"guang-jer-wu",fullName:"Guang-Jer Wu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217323/images/8027_n.jpg",biography:null,institutionString:null,institution:null},{id:"148546",title:"Dr.",name:"Norma Francenia",middleName:null,surname:"Santos-Sánchez",slug:"norma-francenia-santos-sanchez",fullName:"Norma Francenia Santos-Sánchez",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/148546/images/4640_n.jpg",biography:null,institutionString:null,institution:null},{id:"272889",title:"Dr.",name:"Narendra",middleName:null,surname:"Maddu",slug:"narendra-maddu",fullName:"Narendra Maddu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/272889/images/10758_n.jpg",biography:null,institutionString:null,institution:null},{id:"242491",title:"Prof.",name:"Angelica",middleName:null,surname:"Rueda",slug:"angelica-rueda",fullName:"Angelica Rueda",position:"Investigador Cinvestav 3B",profilePictureURL:"https://mts.intechopen.com/storage/users/242491/images/6765_n.jpg",biography:null,institutionString:null,institution:null},{id:"88631",title:"Dr.",name:"Ivan",middleName:null,surname:"Petyaev",slug:"ivan-petyaev",fullName:"Ivan Petyaev",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Lycotec (United Kingdom)",country:{name:"United Kingdom"}}},{id:"423869",title:"Ms.",name:"Smita",middleName:null,surname:"Rai",slug:"smita-rai",fullName:"Smita Rai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424024",title:"Prof.",name:"Swati",middleName:null,surname:"Sharma",slug:"swati-sharma",fullName:"Swati Sharma",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"439112",title:"MSc.",name:"Touseef",middleName:null,surname:"Fatima",slug:"touseef-fatima",fullName:"Touseef Fatima",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424836",title:"Dr.",name:"Orsolya",middleName:null,surname:"Borsai",slug:"orsolya-borsai",fullName:"Orsolya Borsai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Agricultural Sciences and Veterinary Medicine of Cluj-Napoca",country:{name:"Romania"}}},{id:"422262",title:"Ph.D.",name:"Paola Andrea",middleName:null,surname:"Palmeros-Suárez",slug:"paola-andrea-palmeros-suarez",fullName:"Paola Andrea Palmeros-Suárez",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Guadalajara",country:{name:"Mexico"}}}]}},subseries:{item:{id:"8",type:"subseries",title:"Bioinspired Technology and Biomechanics",keywords:"Bioinspired Systems, Biomechanics, Assistive Technology, Rehabilitation",scope:'Bioinspired technologies take advantage of understanding the actual biological system to provide solutions to problems in several areas. Recently, bioinspired systems have been successfully employing biomechanics to develop and improve assistive technology and rehabilitation devices. The research topic "Bioinspired Technology and Biomechanics" welcomes studies reporting recent advances in bioinspired technologies that contribute to individuals\' health, inclusion, and rehabilitation. Possible contributions can address (but are not limited to) the following research topics: Bioinspired design and control of exoskeletons, orthoses, and prostheses; Experimental evaluation of the effect of assistive devices (e.g., influence on gait, balance, and neuromuscular system); Bioinspired technologies for rehabilitation, including clinical studies reporting evaluations; Application of neuromuscular and biomechanical models to the development of bioinspired technology.',coverUrl:"https://cdn.intechopen.com/series_topics/covers/8.jpg",hasOnlineFirst:!1,hasPublishedBooks:!0,annualVolume:11404,editor:{id:"144937",title:"Prof.",name:"Adriano",middleName:"De Oliveira",surname:"Andrade",slug:"adriano-andrade",fullName:"Adriano Andrade",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRC8QQAW/Profile_Picture_1625219101815",biography:"Dr. Adriano de Oliveira Andrade graduated in Electrical Engineering at the Federal University of Goiás (Brazil) in 1997. He received his MSc and PhD in Biomedical Engineering respectively from the Federal University of Uberlândia (UFU, Brazil) in 2000 and from the University of Reading (UK) in 2005. He completed a one-year Post-Doctoral Fellowship awarded by the DFAIT (Foreign Affairs and International Trade Canada) at the Institute of Biomedical Engineering of the University of New Brunswick (Canada) in 2010. Currently, he is Professor in the Faculty of Electrical Engineering (UFU). He has authored and co-authored more than 200 peer-reviewed publications in Biomedical Engineering. He has been a researcher of The National Council for Scientific and Technological Development (CNPq-Brazil) since 2009. He has served as an ad-hoc consultant for CNPq, CAPES (Coordination for the Improvement of Higher Education Personnel), FINEP (Brazilian Innovation Agency), and other funding bodies on several occasions. He was the Secretary of the Brazilian Society of Biomedical Engineering (SBEB) from 2015 to 2016, President of SBEB (2017-2018) and Vice-President of SBEB (2019-2020). He was the head of the undergraduate program in Biomedical Engineering of the Federal University of Uberlândia (2015 - June/2019) and the head of the Centre for Innovation and Technology Assessment in Health (NIATS/UFU) since 2010. He is the head of the Postgraduate Program in Biomedical Engineering (UFU, July/2019 - to date). He was the secretary of the Parkinson's Disease Association of Uberlândia (2018-2019). Dr. Andrade's primary area of research is focused towards getting information from the neuromuscular system to understand its strategies of organization, adaptation and controlling in the context of motor neuron diseases. His research interests include Biomedical Signal Processing and Modelling, Assistive Technology, Rehabilitation Engineering, Neuroengineering and Parkinson's Disease.",institutionString:null,institution:{name:"Federal University of Uberlândia",institutionURL:null,country:{name:"Brazil"}}},editorTwo:null,editorThree:null,series:{id:"7",title:"Biomedical Engineering",doi:"10.5772/intechopen.71985",issn:"2631-5343"},editorialBoard:[{id:"49517",title:"Prof.",name:"Hitoshi",middleName:null,surname:"Tsunashima",slug:"hitoshi-tsunashima",fullName:"Hitoshi Tsunashima",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002aYTP4QAO/Profile_Picture_1625819726528",institutionString:null,institution:{name:"Nihon University",institutionURL:null,country:{name:"Japan"}}},{id:"425354",title:"Dr.",name:"Marcus",middleName:"Fraga",surname:"Vieira",slug:"marcus-vieira",fullName:"Marcus Vieira",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00003BJSgIQAX/Profile_Picture_1627904687309",institutionString:null,institution:{name:"Universidade Federal de Goiás",institutionURL:null,country:{name:"Brazil"}}},{id:"196746",title:"Dr.",name:"Ramana",middleName:null,surname:"Vinjamuri",slug:"ramana-vinjamuri",fullName:"Ramana Vinjamuri",profilePictureURL:"https://mts.intechopen.com/storage/users/196746/images/system/196746.jpeg",institutionString:"University of Maryland, Baltimore County",institution:{name:"University of Maryland, Baltimore County",institutionURL:null,country:{name:"United States of America"}}}]},onlineFirstChapters:{paginationCount:0,paginationItems:[]},publishedBooks:{paginationCount:6,paginationItems:[{type:"book",id:"9008",title:"Vitamin K",subtitle:"Recent Topics on the Biology and Chemistry",coverURL:"https://cdn.intechopen.com/books/images_new/9008.jpg",slug:"vitamin-k-recent-topics-on-the-biology-and-chemistry",publishedDate:"March 23rd 2022",editedByType:"Edited by",bookSignature:"Hiroyuki Kagechika and Hitoshi Shirakawa",hash:"8b43add5389ba85743e0a9491e4b9943",volumeInSeries:27,fullTitle:"Vitamin K - Recent Topics on the Biology and Chemistry",editors:[{id:"180528",title:"Dr.",name:"Hiroyuki",middleName:null,surname:"Kagechika",slug:"hiroyuki-kagechika",fullName:"Hiroyuki Kagechika",profilePictureURL:"https://mts.intechopen.com/storage/users/180528/images/system/180528.jpg",institutionString:"Tokyo Medical and Dental University",institution:{name:"Tokyo Medical and Dental University",institutionURL:null,country:{name:"Japan"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null},{type:"book",id:"9759",title:"Vitamin E in Health and Disease",subtitle:"Interactions, Diseases and Health Aspects",coverURL:"https://cdn.intechopen.com/books/images_new/9759.jpg",slug:"vitamin-e-in-health-and-disease-interactions-diseases-and-health-aspects",publishedDate:"October 6th 2021",editedByType:"Edited by",bookSignature:"Pınar Erkekoglu and Júlia Scherer Santos",hash:"6c3ddcc13626110de289b57f2516ac8f",volumeInSeries:22,fullTitle:"Vitamin E in Health and Disease - Interactions, Diseases and Health Aspects",editors:[{id:"109978",title:"Prof.",name:"Pınar",middleName:null,surname:"Erkekoğlu",slug:"pinar-erkekoglu",fullName:"Pınar Erkekoğlu",profilePictureURL:"https://mts.intechopen.com/storage/users/109978/images/system/109978.jpg",institutionString:"Hacettepe University",institution:{name:"Hacettepe University",institutionURL:null,country:{name:"Turkey"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null},{type:"book",id:"7004",title:"Metabolomics",subtitle:"New Insights into Biology and Medicine",coverURL:"https://cdn.intechopen.com/books/images_new/7004.jpg",slug:"metabolomics-new-insights-into-biology-and-medicine",publishedDate:"July 1st 2020",editedByType:"Edited by",bookSignature:"Wael N. 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Fungal infectious illness prevalence and prognosis are determined by the exposure between fungi and host, host immunological state, fungal virulence, and early and accurate diagnosis and treatment. \r\nPatients with both congenital and acquired immunodeficiency are more likely to be infected with opportunistic mycosis. Fungal infectious disease outbreaks are common during the post- disaster rebuilding era, which is characterised by high population density, migration, and poor health and medical conditions.\r\nSystemic or local fungal infection is mainly associated with the fungi directly inhaled or inoculated in the environment during the disaster. The most common fungal infection pathways are human to human (anthropophilic), animal to human (zoophilic), and environment to human (soilophile). Diseases are common as a result of widespread exposure to pathogenic fungus dispersed into the environment. \r\nFungi that are both common and emerging are intertwined. In Southeast Asia, for example, Talaromyces marneffei is an important pathogenic thermally dimorphic fungus that causes systemic mycosis. Widespread fungal infections with complicated and variable clinical manifestations, such as Candida auris infection resistant to several antifungal medicines, Covid-19 associated with Trichoderma, and terbinafine resistant dermatophytosis in India, are among the most serious disorders. \r\nInappropriate local or systemic use of glucocorticoids, as well as their immunosuppressive effects, may lead to changes in fungal infection spectrum and clinical characteristics. Hematogenous candidiasis is a worrisome issue that affects people all over the world, particularly ICU patients. CARD9 deficiency and fungal infection have been major issues in recent years. Invasive aspergillosis is associated with a significant death rate. Special attention should be given to endemic fungal infections, identification of important clinical fungal infections advanced in yeasts, filamentous fungal infections, skin mycobiome and fungal genomes, and immunity to fungal infections.\r\nIn addition, endemic fungal diseases or uncommon fungal infections caused by Mucor irregularis, dermatophytosis, Malassezia, cryptococcosis, chromoblastomycosis, coccidiosis, blastomycosis, histoplasmosis, sporotrichosis, and other fungi, should be monitored. \r\nThis topic includes the research progress on the etiology and pathogenesis of fungal infections, new methods of isolation and identification, rapid detection, drug sensitivity testing, new antifungal drugs, schemes and case series reports. It will provide significant opportunities and support for scientists, clinical doctors, mycologists, antifungal drug researchers, public health practitioners, and epidemiologists from all over the world to share new research, ideas and solutions to promote the development and progress of medical mycology.",coverUrl:"https://cdn.intechopen.com/series_topics/covers/4.jpg",keywords:"Emerging Fungal Pathogens, Invasive Infections, Epidemiology, Cell Membrane, Fungal Virulence, Diagnosis, Treatment"},{id:"5",title:"Parasitic Infectious Diseases",scope:"Parasitic diseases have evolved alongside their human hosts. In many cases, these diseases have adapted so well that they have developed efficient resilience methods in the human host and can live in the host for years. Others, particularly some blood parasites, can cause very acute diseases and are responsible for millions of deaths yearly. Many parasitic diseases are classified as neglected tropical diseases because they have received minimal funding over recent years and, in many cases, are under-reported despite the critical role they play in morbidity and mortality among human and animal hosts. The current topic, Parasitic Infectious Diseases, in the Infectious Diseases Series aims to publish studies on the systematics, epidemiology, molecular biology, genomics, pathogenesis, genetics, and clinical significance of parasitic diseases from blood borne to intestinal parasites as well as zoonotic parasites. We hope to cover all aspects of parasitic diseases to provide current and relevant research data on these very important diseases. In the current atmosphere of the Coronavirus pandemic, communities around the world, particularly those in different underdeveloped areas, are faced with the growing challenges of the high burden of parasitic diseases. At the same time, they are faced with the Covid-19 pandemic leading to what some authors have called potential syndemics that might worsen the outcome of such infections. Therefore, it is important to conduct studies that examine parasitic infections in the context of the coronavirus pandemic for the benefit of all communities to help foster more informed decisions for the betterment of human and animal health.",coverUrl:"https://cdn.intechopen.com/series_topics/covers/5.jpg",keywords:"Blood Borne Parasites, Intestinal Parasites, Protozoa, Helminths, Arthropods, Water Born Parasites, Epidemiology, Molecular Biology, Systematics, Genomics, Proteomics, Ecology"},{id:"6",title:"Viral Infectious Diseases",scope:"The Viral Infectious Diseases Book Series aims to provide a comprehensive overview of recent research trends and discoveries in various viral infectious diseases emerging around the globe. The emergence of any viral disease is hard to anticipate, which often contributes to death. A viral disease can be defined as an infectious disease that has recently appeared within a population or exists in nature with the rapid expansion of incident or geographic range. This series will focus on various crucial factors related to emerging viral infectious diseases, including epidemiology, pathogenesis, host immune response, clinical manifestations, diagnosis, treatment, and clinical recommendations for managing viral infectious diseases, highlighting the recent issues with future directions for effective therapeutic strategies.",coverUrl:"https://cdn.intechopen.com/series_topics/covers/6.jpg",keywords:"Novel Viruses, Virus Transmission, Virus Evolution, Molecular Virology, Control and Prevention, Virus-host Interaction"}],annualVolumeBook:{},thematicCollection:[],selectedSeries:null,selectedSubseries:null},seriesLanding:{item:{id:"11",title:"Biochemistry",doi:"10.5772/intechopen.72877",issn:"2632-0983",scope:"Biochemistry, the study of chemical transformations occurring within living organisms, impacts all areas of life sciences, from molecular crystallography and genetics to ecology, medicine, and population biology. Biochemistry examines macromolecules - proteins, nucleic acids, carbohydrates, and lipids – and their building blocks, structures, functions, and interactions. Much of biochemistry is devoted to enzymes, proteins that catalyze chemical reactions, enzyme structures, mechanisms of action and their roles within cells. Biochemistry also studies small signaling molecules, coenzymes, inhibitors, vitamins, and hormones, which play roles in life processes. Biochemical experimentation, besides coopting classical chemistry methods, e.g., chromatography, adopted new techniques, e.g., X-ray diffraction, electron microscopy, NMR, radioisotopes, and developed sophisticated microbial genetic tools, e.g., auxotroph mutants and their revertants, fermentation, etc. More recently, biochemistry embraced the ‘big data’ omics systems. Initial biochemical studies have been exclusively analytic: dissecting, purifying, and examining individual components of a biological system; in the apt words of Efraim Racker (1913 –1991), “Don’t waste clean thinking on dirty enzymes.” Today, however, biochemistry is becoming more agglomerative and comprehensive, setting out to integrate and describe entirely particular biological systems. The ‘big data’ metabolomics can define the complement of small molecules, e.g., in a soil or biofilm sample; proteomics can distinguish all the comprising proteins, e.g., serum; metagenomics can identify all the genes in a complex environment, e.g., the bovine rumen. This Biochemistry Series will address the current research on biomolecules and the emerging trends with great promise.",coverUrl:"https://cdn.intechopen.com/series/covers/11.jpg",latestPublicationDate:"May 15th, 2022",hasOnlineFirst:!0,numberOfOpenTopics:4,numberOfPublishedChapters:286,numberOfPublishedBooks:27,editor:{id:"31610",title:"Dr.",name:"Miroslav",middleName:null,surname:"Blumenberg",fullName:"Miroslav Blumenberg",profilePictureURL:"https://mts.intechopen.com/storage/users/31610/images/system/31610.jpg",biography:"Miroslav Blumenberg, Ph.D., was born in Subotica and received his BSc in Belgrade, Yugoslavia. He completed his Ph.D. at MIT in Organic Chemistry; he followed up his Ph.D. with two postdoctoral study periods at Stanford University. Since 1983, he has been a faculty member of the RO Perelman Department of Dermatology, NYU School of Medicine, where he is codirector of a training grant in cutaneous biology. Dr. Blumenberg’s research is focused on the epidermis, expression of keratin genes, transcription profiling, keratinocyte differentiation, inflammatory diseases and cancers, and most recently the effects of the microbiome on the skin. He has published more than 100 peer-reviewed research articles and graduated numerous Ph.D. and postdoctoral students.",institutionString:null,institution:{name:"New York University Langone Medical Center",institutionURL:null,country:{name:"United States of America"}}},subseries:[{id:"14",title:"Cell and Molecular Biology",keywords:"Omics (Transcriptomics; Proteomics; Metabolomics), Molecular Biology, Cell Biology, Signal Transduction and Regulation, Cell Growth and Differentiation, Apoptosis, Necroptosis, Ferroptosis, Autophagy, Cell Cycle, Macromolecules and Complexes, Gene Expression",scope:"The Cell and Molecular Biology topic within the IntechOpen Biochemistry Series aims to rapidly publish contributions on all aspects of cell and molecular biology, including aspects related to biochemical and genetic research (not only in humans but all living beings). We encourage the submission of manuscripts that provide novel and mechanistic insights that report significant advances in the fields. Topics include, but are not limited to: Advanced techniques of cellular and molecular biology (Molecular methodologies, imaging techniques, and bioinformatics); Biological activities at the molecular level; Biological processes of cell functions, cell division, senescence, maintenance, and cell death; Biomolecules interactions; Cancer; Cell biology; Chemical biology; Computational biology; Cytochemistry; Developmental biology; Disease mechanisms and therapeutics; DNA, and RNA metabolism; Gene functions, genetics, and genomics; Genetics; Immunology; Medical microbiology; Molecular biology; Molecular genetics; Molecular processes of cell and organelle dynamics; Neuroscience; Protein biosynthesis, degradation, and functions; Regulation of molecular interactions in a cell; Signalling networks and system biology; Structural biology; Virology and microbiology.",annualVolume:11410,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/14.jpg",editor:{id:"165627",title:"Dr.",name:"Rosa María",middleName:null,surname:"Martínez-Espinosa",fullName:"Rosa María Martínez-Espinosa",profilePictureURL:"https://mts.intechopen.com/storage/users/165627/images/system/165627.jpeg",institutionString:null,institution:{name:"University of Alicante",institutionURL:null,country:{name:"Spain"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"79367",title:"Dr.",name:"Ana Isabel",middleName:null,surname:"Flores",fullName:"Ana Isabel Flores",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRpIOQA0/Profile_Picture_1632418099564",institutionString:null,institution:{name:"Hospital Universitario 12 De Octubre",institutionURL:null,country:{name:"Spain"}}},{id:"328234",title:"Ph.D.",name:"Christian",middleName:null,surname:"Palavecino",fullName:"Christian Palavecino",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000030DhEhQAK/Profile_Picture_1628835318625",institutionString:null,institution:{name:"Central University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"186585",title:"Dr.",name:"Francisco Javier",middleName:null,surname:"Martin-Romero",fullName:"Francisco Javier Martin-Romero",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSB3HQAW/Profile_Picture_1631258137641",institutionString:null,institution:{name:"University of Extremadura",institutionURL:null,country:{name:"Spain"}}}]},{id:"15",title:"Chemical Biology",keywords:"Phenolic Compounds, Essential Oils, Modification of Biomolecules, Glycobiology, Combinatorial Chemistry, Therapeutic peptides, Enzyme Inhibitors",scope:"Chemical biology spans the fields of chemistry and biology involving the application of biological and chemical molecules and techniques. In recent years, the application of chemistry to biological molecules has gained significant interest in medicinal and pharmacological studies. This topic will be devoted to understanding the interplay between biomolecules and chemical compounds, their structure and function, and their potential applications in related fields. Being a part of the biochemistry discipline, the ideas and concepts that have emerged from Chemical Biology have affected other related areas. This topic will closely deal with all emerging trends in this discipline.",annualVolume:11411,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/15.jpg",editor:{id:"441442",title:"Dr.",name:"Şükrü",middleName:null,surname:"Beydemir",fullName:"Şükrü Beydemir",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00003GsUoIQAV/Profile_Picture_1634557147521",institutionString:null,institution:{name:"Anadolu University",institutionURL:null,country:{name:"Turkey"}}},editorTwo:{id:"13652",title:"Prof.",name:"Deniz",middleName:null,surname:"Ekinci",fullName:"Deniz Ekinci",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002aYLT1QAO/Profile_Picture_1634557223079",institutionString:null,institution:{name:"Ondokuz Mayıs University",institutionURL:null,country:{name:"Turkey"}}},editorThree:null,editorialBoard:[{id:"241413",title:"Dr.",name:"Azhar",middleName:null,surname:"Rasul",fullName:"Azhar Rasul",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRT1oQAG/Profile_Picture_1635251978933",institutionString:null,institution:{name:"Government College University, Faisalabad",institutionURL:null,country:{name:"Pakistan"}}},{id:"178316",title:"Ph.D.",name:"Sergey",middleName:null,surname:"Sedykh",fullName:"Sergey Sedykh",profilePictureURL:"https://mts.intechopen.com/storage/users/178316/images/system/178316.jfif",institutionString:null,institution:{name:"Novosibirsk State University",institutionURL:null,country:{name:"Russia"}}}]},{id:"17",title:"Metabolism",keywords:"Biomolecules Metabolism, Energy Metabolism, Metabolic Pathways, Key Metabolic Enzymes, Metabolic Adaptation",scope:"Metabolism is frequently defined in biochemistry textbooks as the overall process that allows living systems to acquire and use the free energy they need for their vital functions or the chemical processes that occur within a living organism to maintain life. Behind these definitions are hidden all the aspects of normal and pathological functioning of all processes that the topic ‘Metabolism’ will cover within the Biochemistry Series. Thus all studies on metabolism will be considered for publication.",annualVolume:11413,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/17.jpg",editor:{id:"138626",title:"Dr.",name:"Yannis",middleName:null,surname:"Karamanos",fullName:"Yannis Karamanos",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002g6Jv2QAE/Profile_Picture_1629356660984",institutionString:null,institution:{name:"Artois University",institutionURL:null,country:{name:"France"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"243049",title:"Dr.",name:"Anca",middleName:null,surname:"Pantea Stoian",fullName:"Anca Pantea Stoian",profilePictureURL:"https://mts.intechopen.com/storage/users/243049/images/system/243049.jpg",institutionString:null,institution:{name:"Carol Davila University of Medicine and Pharmacy",institutionURL:null,country:{name:"Romania"}}},{id:"203824",title:"Dr.",name:"Attilio",middleName:null,surname:"Rigotti",fullName:"Attilio Rigotti",profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institutionString:null,institution:{name:"Pontifical Catholic University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"300470",title:"Dr.",name:"Yanfei (Jacob)",middleName:null,surname:"Qi",fullName:"Yanfei (Jacob) Qi",profilePictureURL:"https://mts.intechopen.com/storage/users/300470/images/system/300470.jpg",institutionString:null,institution:{name:"Centenary Institute of Cancer Medicine and Cell Biology",institutionURL:null,country:{name:"Australia"}}}]},{id:"18",title:"Proteomics",keywords:"Mono- and Two-Dimensional Gel Electrophoresis (1-and 2-DE), Liquid Chromatography (LC), Mass Spectrometry/Tandem Mass Spectrometry (MS; MS/MS), Proteins",scope:"With the recognition that the human genome cannot provide answers to the etiology of a disorder, changes in the proteins expressed by a genome became a focus in research. Thus proteomics, an area of research that detects all protein forms expressed in an organism, including splice isoforms and post-translational modifications, is more suitable than genomics for a comprehensive understanding of the biochemical processes that govern life. The most common proteomics applications are currently in the clinical field for the identification, in a variety of biological matrices, of biomarkers for diagnosis and therapeutic intervention of disorders. From the comparison of proteomic profiles of control and disease or different physiological states, which may emerge, changes in protein expression can provide new insights into the roles played by some proteins in human pathologies. Understanding how proteins function and interact with each other is another goal of proteomics that makes this approach even more intriguing. Specialized technology and expertise are required to assess the proteome of any biological sample. Currently, proteomics relies mainly on mass spectrometry (MS) combined with electrophoretic (1 or 2-DE-MS) and/or chromatographic techniques (LC-MS/MS). MS is an excellent tool that has gained popularity in proteomics because of its ability to gather a complex body of information such as cataloging protein expression, identifying protein modification sites, and defining protein interactions. The Proteomics topic aims to attract contributions on all aspects of MS-based proteomics that, by pushing the boundaries of MS capabilities, may address biological problems that have not been resolved yet.",annualVolume:11414,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/18.jpg",editor:{id:"200689",title:"Prof.",name:"Paolo",middleName:null,surname:"Iadarola",fullName:"Paolo Iadarola",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSCl8QAG/Profile_Picture_1623568118342",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorTwo:{id:"201414",title:"Dr.",name:"Simona",middleName:null,surname:"Viglio",fullName:"Simona Viglio",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRKDHQA4/Profile_Picture_1630402531487",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorThree:null,editorialBoard:[{id:"72288",title:"Dr.",name:"Arli Aditya",middleName:null,surname:"Parikesit",fullName:"Arli Aditya Parikesit",profilePictureURL:"https://mts.intechopen.com/storage/users/72288/images/system/72288.jpg",institutionString:null,institution:{name:"Indonesia International Institute for Life Sciences",institutionURL:null,country:{name:"Indonesia"}}},{id:"40928",title:"Dr.",name:"Cesar",middleName:null,surname:"Lopez-Camarillo",fullName:"Cesar Lopez-Camarillo",profilePictureURL:"https://mts.intechopen.com/storage/users/40928/images/3884_n.png",institutionString:null,institution:{name:"Universidad Autónoma de la Ciudad de México",institutionURL:null,country:{name:"Mexico"}}},{id:"81926",title:"Dr.",name:"Shymaa",middleName:null,surname:"Enany",fullName:"Shymaa Enany",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRqB9QAK/Profile_Picture_1626163237970",institutionString:null,institution:{name:"Suez Canal University",institutionURL:null,country:{name:"Egypt"}}}]}]}},libraryRecommendation:{success:null,errors:{},institutions:[]},route:{name:"profile.detail",path:"/profiles/415286",hash:"",query:{},params:{id:"415286"},fullPath:"/profiles/415286",meta:{},from:{name:null,path:"/",hash:"",query:{},params:{},fullPath:"/",meta:{}}}},function(){var e;(e=document.currentScript||document.scripts[document.scripts.length-1]).parentNode.removeChild(e)}()