\\n\\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 191 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 261 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
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\r\n\r\n\tThe book aims to provide a clear presentation of the concepts, tools, and applications of the field of Product Life Cycle in the sustainable and digital transformation perspective. The main topics characterizing Product Life Cycle including both managerial issues and practical applications will be considered.
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He has authored/co-authored numerous articles in the areas of decision science and business management and is a member of editorial boards of several international organizations and journals.",coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"181603",title:"Dr.",name:"Antonella",middleName:null,surname:"Petrillo",slug:"antonella-petrillo",fullName:"Antonella Petrillo",profilePictureURL:"https://mts.intechopen.com/storage/users/181603/images/system/181603.jpeg",biography:"Antonella Petrillo is a Professor at the Department of Engineering of the University of Naples 'Parthenope”, Italy. She received her Ph.D. in Mechanical Engineering from the University of Cassino. Her research interests include multi-criteria decision analysis, sustainability, logistics, manufacturing and safety. She serves as an Associate Editor for the International Journal of the Analytic Hierarchy Process. She is a member of AHP Academy and a member of several editorial boards.",institutionString:"Parthenope University of Naples",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"7",totalChapterViews:"0",totalEditedBooks:"3",institution:{name:"Parthenope University of Naples",institutionURL:null,country:{name:"Italy"}}}],coeditorOne:{id:"161682",title:"Prof.",name:"Fabio",middleName:null,surname:"De Felice",slug:"fabio-de-felice",fullName:"Fabio De Felice",profilePictureURL:"https://mts.intechopen.com/storage/users/161682/images/system/161682.jpeg",biography:"Fabio De Felice is a Professor at the University of Cassino and Southern Lazio, Italy, where he received his Ph.D. in Mechanical Engineering. His current research focuses on multi-criteria decision-making analysis (with an emphasis on AHP and ANP) and industrial, project and supply chain management. Currently, he serves as a member of the Scientific Advisory Committee of the International Symposium on the Analytic Hierarchy Process (ISAHP). He is the founder of AHP Academy that promotes the diffusion of the culture and methodologies of Decision Making, with particular reference to those based on the Analytic Hierarchy Process. He is a member of the editorial boards of several international organizations and journals and has authored/co-authored numerous articles in the areas of decision science and business management.",institutionString:"University of Cassino and Southern Lazio Lazio",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"5",totalChapterViews:"0",totalEditedBooks:"2",institution:{name:"University of Cassino and Southern Lazio",institutionURL:null,country:{name:"Italy"}}},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:"345821",firstName:"Darko",lastName:"Hrvojic",middleName:null,title:"Mr.",imageUrl:"https://mts.intechopen.com/storage/users/345821/images/16410_n.",email:"darko@intechopen.com",biography:null}},relatedBooks:[{type:"book",id:"6291",title:"Digital Transformation in Smart Manufacturing",subtitle:null,isOpenForSubmission:!1,hash:"0a889d0839f7d4e2639d44c429a20906",slug:"digital-transformation-in-smart-manufacturing",bookSignature:"Antonella Petrillo, Raffaele Cioffi and Fabio De Felice",coverURL:"https://cdn.intechopen.com/books/images_new/6291.jpg",editedByType:"Edited by",editors:[{id:"181603",title:"Dr.",name:"Antonella",surname:"Petrillo",slug:"antonella-petrillo",fullName:"Antonella Petrillo"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"8264",title:"New Frontiers on Life Cycle Assessment",subtitle:"Theory and Application",isOpenForSubmission:!1,hash:"59f13958eb30b72de4f8d1bc63f6dd2d",slug:"new-frontiers-on-life-cycle-assessment-theory-and-application",bookSignature:"Antonella Petrillo and Fabio De Felice",coverURL:"https://cdn.intechopen.com/books/images_new/8264.jpg",editedByType:"Edited by",editors:[{id:"181603",title:"Dr.",name:"Antonella",surname:"Petrillo",slug:"antonella-petrillo",fullName:"Antonella Petrillo"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"10020",title:"Operations Management",subtitle:"Emerging Trend in the Digital Era",isOpenForSubmission:!1,hash:"526f0dbdc7e4d85b82ce8383ab894b4c",slug:"operations-management-emerging-trend-in-the-digital-era",bookSignature:"Antonella Petrillo, Fabio De Felice, Germano Lambert-Torres and Erik Bonaldi",coverURL:"https://cdn.intechopen.com/books/images_new/10020.jpg",editedByType:"Edited by",editors:[{id:"181603",title:"Dr.",name:"Antonella",surname:"Petrillo",slug:"antonella-petrillo",fullName:"Antonella Petrillo"}],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:"Theophanides",surname:"Theophile",slug:"theophanides-theophile",fullName:"Theophanides Theophile"}],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"}}]},chapter:{item:{type:"chapter",id:"57736",title:"The Role of Erythropoietin-Derived Peptides in Tissue Protection",doi:"10.5772/intechopen.71931",slug:"the-role-of-erythropoietin-derived-peptides-in-tissue-protection",body:'\nTissue injury refers to the histologic lesions and the subsequent functional insufficiencies of tissues and organs that are caused by multiple sources, such as ischemia followed by reperfusion [1], trauma [2], autoimmune inflammation [3], oxidative stress [4], drugs and toxicants [5], etc. In histology, it is characterized by the infiltration of pro-inflammatory cells and cytokines and the cellular necrosis and apoptosis induced by damage-associated molecular patterns [6, 7]. Considering the high morbidity and mortality it has caused, the protection from tissue injury is a major concern in the basic and clinical medical academies worldwide. Erythropoietin (EPO), recognized as the erythropoietic hormone secreted in response to anemia, was reported to trigger anti-inflammatory and anti-apoptotic processes to attenuate tissue injury and promote the repairing of injured tissues by binding to tissue protective erythropoietin receptor (EPOR)/β common receptor (βcR) heterodimer [8]. However, only at a high dosage can EPO exert tissue protective effects, which simultaneously elicits some severe erythropoiesis-related side effects [9]. Thus, the structural modification of EPO for the prevention of side effects is undoubtedly required. This chapter reviewed the development from EPO to its peptide derivatives with tissue protective efficacy. Also discussed are the therapeutic effects and limitations of each peptide, signaling pathways involved and the benefits for translation.
\nEPO is a glycoprotein hormone, which is predominately produced and secreted by the adult kidney in response to anemia [10, 11]. After sensing the hypoxic signal in anemic conditions, the fibroblasts in the interstitial area of the renal cortex are activated to produce EPO [12, 13]. EPO stimulates erythropoiesis through binding to its EPOR expressed on the surface of the red blood cell progenitors and precursors in bone marrow [14, 15]. In normal conditions, the level of erythropoietin in the blood is quite low [10]. Under hypoxic stress, however, EPO production may be increased up to 1000-fold, reaching 10,000 mU/ml in the blood [13]. In structure, EPO consists of four long alpha-helixes (A, B, C, and D) running in an up-up-down-down direction, connected by two long cross-over loops (AB and CD) and one short loop (BC). Among the four helixes, only helix A, C, and helix D and the loop connecting helix A and B within the dimensional structure are essential for interacting with EPOR, while helix B faces away from the interior of the receptor in the tertiary structure [13, 16, 17, 18].
\nDuring the past decade, greater interest has been paid to the pleiotropic biologic actions of EPO beyond the stimulation of erythropoiesis, which include anti-apoptosis, anti-inflammation, neurogenesis, and angiogenesis, as well as their consequent tissue protection [8, 19, 20, 21]. An increasing body of studies demonstrated that EPO exerts a powerful tissue-protective effect on a variety of organs and can prevent cellular apoptosis from some sources, including reduced or absent oxygen tension, ischemia–reperfusion, toxicity and free radical exposure. Our study in a murine model of renal injury showed that EPO protected kidneys against injury through decreasing positive myeloperoxidase neutrophils and suppressing the expression of pro-inflammatory cytokines and chemokines by the inhibition of NF-kB signaling pathway [22]. In the study with isolated porcine renal allografts, it was demonstrated that EPO promoted inflammatory cell apoptosis, drove inflammatory and apoptotic cells into tubular lumens, thereby leading to inflammation clearance in the involved tissue and organs [23]. We also reported in our recent study that EPO could affect the dynamics of macrophages in the model of rhabdomyolysis-induced acute kidney injury. In this study, EPO was found to ameliorate kidney injury by reducing macrophages recruitment and promoting phenotype switch from M1 to M2 [24]. In vitro study, EPO was shown to directly suppress pro-inflammatory responses of M1 macrophages and promote M2 marker expression [24]. These results refreshed our understanding about the immunoregulatory capacity of EPO.
\nThe mechanisms involved in the tissue protective effect of EPO was not well illustrated until the specific receptor mediating tissue protection was revealed, which was recently defined as a heterodimer composed of EPOR and CD131 [25]. CD131 also forms the receptor complexes with α receptor subunits specific for GM-CSF, IL-3, and IL-5 and thus is named as β common receptor [25]. In aqueous media, helix B and parts of the AB and CD loops face the aqueous medium but away from the erythropoietic binding sites, which indicates that helix B mediates tissue protective effect of EPO via binding with EPOR/βcR heterodimer [26]. Following the interaction of EPO with EPOR/βcR, the Akt involved signaling pathway is reported to play a vital role in mediating intracellular signal transduction. The activation of PI3K/Akt pathway by EPO maintains the mitochondrial membrane integrity, prevents cytochrome C from release and modulates the activity of caspase cascade during cellular apoptosis [27, 28]. The blockade of Akt phosphorylation abrogates the anti-apoptotic and anti-inflammatory effect after EPO administration [28, 29]. Moreover, the activation of Akt after EPO treatment is also reported to protect against genomic DNA degradation and membrane phosphatidylserine exposure [28, 30]. Several transcriptional modulators in the downstream pathways of Akt have also been shown to mediate the tissue-protection of EPO. For example, EPO could down-regulate the activity of forkhead transcription factor (FOXO3a) through inhibitory phosphorylation, which renders FOXO3a ineffective to activate the transcription of nuclear genes involved in apoptosis [31]. Other mechanisms include the inhibition of glycogen synthase kinase-3β [32], a serine-threonine kinase that plays a significant role in the induction of apoptosis of neurons, vascular smooth muscle cells and cardiomyocytes, and the up-regulation of the anti-apoptotic Bcl-2 family member Bcl-xL [33].
\nThe role of EPO in anti-inflammation and anti-apoptosis inspired us to investigate if EPO could also be served as a potential therapy for tissue injury caused by the exposure to drugs, chemicals, or physical ischemia. However, the tissue protective effect of EPO only occurs at the dosage that is well above normal, which may simultaneously elicit severe side-effects associated with its erythropoietic effects such as polycythemia and hypercoagulation in the circulation [9]. The demand of high dose to exert the tissue protective activities may be caused by the relatively low affinity of EPO to the tissue-protective EPOR/βcR dimer receptor relative to the erythropoietic (EPOR)2 homodimer [15, 20, 34]. Being enlightened by the finding that helix B plays a dominant role in mediating the tissue protective effect by binding with EPOR/βcR receptor, Michael Brines et al. first synthesized the nonerythropoietic, tissue-protective peptides derived from the tertiary structure of erythropoietin which comprises the amino acid sequence corresponding to helix B as well as the three residues within the proximal portion of the BC loop. The design of the novel peptide aims to mimic the three-dimensional structure that interacts with EPOR/βcR receptor to reproduce the tissue-protective activities of the full molecule [26]. This 11-mer peptide derivative was named as helix B surface peptide (HBSP) [26]. Following studies demonstrated that HBSP is sufficient to activate tissue-protective pathways representative of the full molecule and protect from injury in a wide variety of tissues and organs but without causing erythropoietic effects.
\nHBSP was demonstrated to exert tissue protective effects first in the cardiovascular system after it was designed. The designers of this peptide showed that HBSP protected cardiomyocytes from TNF-α apoptosis in an Akt-dependent pathway both in vitro and in vivo [26, 35]. In this study, the levels of serum creatinine kinase activity and of cardiac expression of atrial natriuretic peptide, a marker of chronic heart failure, were down-regulated in animals treated with HBSP [26, 35]. Then, the anti-atherosclerotic effects HBSP were investigated in vitro and in vivo [36]. In vitro, HBSP inhibited C-reactive protein induced apoptosis in human umbilical vein endothelial cells and THP-1 cells to a great extent [36]. In the hyperlipidemic spontaneous myocardial infarction model of rabbits, HBSP was shown to significantly suppress the progression of coronary stenosis and myocardial ischemia caused by atherosclerotic lesions and inhibit coronary artery endothelial cell apoptosis through the activation of Akt pathway and the corresponding decreased the production of TNF-α as well as modified macrophage M1/M2 polarization [36]. Similarly, in the myocardial ischemia-reperfusion injury model of mice, HBSP administration before reperfusion significantly reduced the myocardial infarct size, decreased cardiomyocyte apoptosis, reduced the activities of superoxide dismutase and partially preserved heart function through the upregulation of Akt/GSK-3β/ERK and STAT-3 [37]. In an in vitro study performed by using a rodent cardiomyocyte cell line subjected to hypoxia-reoxygenation injury, HBSP was reported to have protective effects by reducing cellular apoptosis, mitochondrial reactive oxygen production, ΔΨm collapse, and cytochrome C release from mitochondria to the cytosol. Furthermore, HBSP inhibited the activation of caspase 9 and caspase 3 as well as the alteration of Bcl-2 family proteins induced by hypoxia-reoxygenation [38]. Diabetes is also one of the major causes of myocardial lesions. Diabetic cardiomyopathy (DCM) is a ventricular dysfunction independent of coronary artery disease and hypertension, which is associated with inflammation, myocardial apoptosis and fibrosis [39, 40, 41]. In a study regarding the protection of HBSP on DCM, HBSP notably improved cardiac function, attenuated cardiac interstitial fibrosis, inhibited myocardial apoptosis, and ameliorated mitochondrial ultrastructure in mice with diabetic cardiomyopathy through an AMPK-dependent pathway [42]. HBSP promoted aortic endothelial cell repair under hypoxic conditions in a model of aortic endothelial injury, in which HBSP enhanced scratch closure by promoting cell migration and proliferation [43]. Furthermore, EPO protected bovine aortic endothelial cells from staurosporine-induced apoptosis under hypoxic conditions. Hypoxia was associated with a reduction in nitric oxide (NO) production. HBSP notably increased NO production, in a manner sensitive to NO synthase inhibition, under hypoxic conditions but not under normoxic conditions [43]. In summary, multiple studies proved the protective effect of HBSP on myocardial tissues and endothelial cells in the cardiovascular system following the injury caused by insufficient oxygen supply and implied that Akt pathway played a critical role in this process.
\nAnother field of research in which the protection of HBSP was well investigated is in the nervous system. In one study by Robertson et al., the effects of HBSP on early cerebral hemodynamics and neurological outcome post-injury were investigated in a rat model of mild cortical impact injury followed hemorrhagic hypotension [44]. The results demonstrated that both EPO and HBSP treated groups improved recovery of cerebral blood flow in the injured brain following resuscitation, and showed more rapid recovery in the performance of functional neural tests. This study suggests that HBSP has neuroprotective effects similar to EPO in this model of combined brain injury and hypotension [44]. They later reported that the treatment with HBSP resulted in significantly improved performance after the rats were suffered from mild traumatic brain injury (mTBI), which was associated with decreased infiltration of CD68-positive inflammatory cells in the damaged brain tissue [45]. The results suggest that HBSP may improve cognitive function following mTBI [45]. Among the patients with neuritis, neuropathic pain is a quite common symptom, which may be due to nerve inflammation. The neuropathic pain results from several overlapping pathways, which then merges into a magnified pain status with symptoms such as allodynia and hyperalgesia [46, 47]. The study by Pulman KG et al., examined the effects of HBSP on pain behavior in the rat model of neuritis [48]. The results showed that treatment with HBSP prevented the development of mechanical allodynia caused by neuritis but not affect heat hyperalgesia [48]. In another study, HBSP treatment could reduce allodynia coupled to the suppression of spinal microglia response in a dose-dependent manner, which may result from HBSP-induced suppression of inflammation in central nervous system [49]. In the study on the therapeutic effects of HBSP in experimental autoimmune encephalomyelitis (EAE), the administration of HBSP to EAE rats significantly reduced the severity and shortened the duration of injury, reduced the infiltration of pro-inflammatory cells and suppressed expression of pro-inflammatory cytokines such as IL-1β, IL-17, TNF-α, IFN-γ. The expression of inducible NO synthase and transcription factor T-bet at mRNA level was also reduced in spinal cords following HBSP treatment [50]. In the in vitro study, HBSP inhibited antigen-specific and non-specific lymphocyte proliferation and promoted the polarization of Th2 and regulatory T cells (Treg) while suppressed the polarization of Th1 and Th17 cells in EAE lymph nodes [50]. In summary, these studies regarding the role of HBSP in nervous system revealed that HBSP could also protect the nervous tissue from injury, which was associated with the alteration of the cytokine and cell milieu to limit inflammation in the damaged nervous tissue.
\nSeveral recent studies focused on the evaluation of the effects and potential mechanisms of HBSP in obesity modulation and diabetes-related disorders. One study was performed by using male C57BL/6 J mice fed with high-fat high-sucrose (HFHS) diet [51]. HFHS diet treated mice exhibited insulin resistance, hyperlipidemia, hepatic lipid accumulation and kidney dysfunction, which was related to the impaired insulin signal pathway and reduced membrane translocation of glucose transporter 4 [51]. However, treatment with HBSP ameliorated renal function, reduced hepatic lipid deposition, and normalized serum glucose and lipid profiles, which were associated with improved insulin sensitivity and glucose uptake in skeletal muscle. The mechanism included that HBSP attenuated the HFHS-induced overproduction of IL-6 and fibroblast growth factor-21, and enhanced mitochondrial biogenesis in skeletal muscle [51]. In another study regarding the effect of HBSP on obesity, HBSP was found to protect against obesity and insulin resistance by suppressing adipogenesis, adipokine expression as well as attenuating macrophage inflammatory activation in lipid tissue [52]. The retinopathy is one of the most common complications of diabetes and remains one of the leading causes of non-congenital blindness [53]. In the diabetic retina, vasodegenerative phase is accompanied by neuroglial abnormalities and eventual depletion of ganglion cells [54]. HBSP was shown to significantly reduce microglial activation and protected against neuroglial and vascular degeneration but without exacerbating neovascularization in the retina [55]. These findings suggest that HBSP has therapeutic implications for metabolic disorders, such as obesity, diabetes, and diabetic retinopathy.
\nOur research mainly discussed the tissue protection of HBSP on kidney injury. In 2013, we investigated effects of HBSP and the expression of EPOR/βcR heterodimer receptor in a murine renal ischemia-reperfusion (IR) injury model [56]. We found that HBSP could significantly ameliorate renal dysfunction and tissue damage, reduced apoptotic cells in the kidney and inhibited the activation of caspase-9 and caspase-3 [56]. The expression of EPOR/βcR in the kidney was up-regulated following ischemia-reperfusion injury but was down-regulated by the treatment of HBSP [56]. Further investigation revealed that the PI3K-Akt pathway was dramatically activated by HBSP. The treatment of the PI3K inhibitor, Wortmannin, abolished improved renal function and histologic structure by HBSP [56]. This study suggests that HBSP could protect the kidney from IR injury in a PI3K-Akt dependent pathway. Then, we also investigated the role of HBSP in IR and cyclosporine A (CsA) induced kidney injury since both of them are unavoidable after kidney transplantation and associated with allograft dysfunction [57]. We found that the level of creatinine and blood urea nitrogen was increased by CsA but decreased by HBSP. HBSP also significantly ameliorated tubulointerstitial damage and interstitial fibrosis, which were gradually increased by IR and CsA [57]. In addition, apoptotic cells, infiltrated inflammatory cells, and active caspase-3 positive cells were greatly reduced by HBSP. It was demonstrated for the first time that HBSP effectively improved renal function and tissue damage caused by IR and/or CsA, which might be through reducing caspase-3 activation and synthesis, apoptosis, and inflammation [57]. Similar findings were also reported by Nimesh SA Patel’s and Willem G van Rijt’s groups that HBSP has renoprotective capacities by anti-inflammation and anti-apoptosis in the injured kidney tissue [58, 59].
\nVery recently, the protective effect of HBSP on acute liver injury was investigated in Wu’s study. In this study, the acute liver injury was induced by the administration of carbon tetrachloride (CCl4) [60]. HBSP was demonstrated to significantly decrease serum alanine aminotransferase, aspartate aminotransferase, lactate dehydrogenase, and pro-inflammatory cytokines in liver tissues after CCl4 injection. The infiltration of CD3, CD8, and CD68 positive cells and the expression of cleaved caspase-3 were also significantly decreased by HBSP treatment. The glutathione peroxidase activity and survival rate increased, while the total apoptotic rate was reduced in the HBSP-treated group. As to the mechanism, the authors reported that HBSP activated the PI3K/Akt/mTORC1 pathway [60]. Thus, HBSP showed convincing protective effects on CCl4-induced acute liver injury by ameliorating inflammation and apoptosis [60].
\nDespite the powerful tissue-protective function exhibited in various organs by inhibiting inflammation and apoptosis, the property of poor permeability to biomembranes, unstable secondary structure, and short half-time restricts the application of HBSP in translation study [26]. Therefore, the structurally optimized transformation of HBSP is urgently required. It is acknowledged that peptide cyclization could provide an efficient strategy to overcome these problems [61]. Provoked by this, we for the first time introduced the head-to-tail cyclization to the structure of HBSP to improve its stability, since the backbone of the peptide was constrained by the cyclization in which the linkages between main chains were formed by thioether [62]. This newly designed and synthesized peptide was named as thioether-cyclized helix B peptide (CHBP) [62].
\nIn the following study, we demonstrate that CHBP is significantly stable in the human plasma and has a 2.5-fold longer half-life time than HBSP, suggesting that CHBP is highly resistant to proteolytic degradation both in vitro and in vivo [63]. We also found in our study that due to its stability, this long-acting peptide could ameliorate renal IR injury to a greater extent than HBSP, for only one dose of CHBP exerted persistent renal protective effect throughout the one week post IR injury [63]. Autophagy is demonstrated to play a renoprotective role in IR injury and is closely related to cellular apoptosis and inflammation in kidney tissue [64]. We also found that CHBP could induce autophagy in the injured kidney by increasing LC3-II/I ratio as well as upregulating beclin-1 [62]. Furthermore, our study depicted possible signaling pathways involved in CHBP-induced autophagy, which included the regulation of mammalian target of rapamycin (mTOR) pathway and the activation of AMPK pathway. The activation of AMPK by CHBP then phosphorylated and activated tuberous sclerosis 2 (TSC2), which connected with tuberous sclerosis 1(TSC1) to form a heterodimer to inhibit the activation of mammalian target of rapamycin complex 1 (mTORC1). Meanwhile, the mTORC2-Akt pathway was activated by CHBP and autophagy was induced by the altered mTORC1/mTORC2 equilibrium [62]. Also, CHBP was reported to upregulate Treg and downregulate helper T cell 17 (Th17) after renal IR injury to restore the Treg/Th17 balance [62]. These findings revealed the mechanisms that are involved in the tissue protective function in CHBP but have not been reported in HBSP yet.
\nDuring the transport of donated organs, any strategies that can effectively protect against IR injury during the cold storage (CS) and reperfusion stages would be very beneficial for preventing the delayed graft function after kidney transplant surgery. Thus, we administrated CHBP in the preservation solution and autologous blood perfusate to examine its effect on the preservation of isolated donor kidney in the following study [65]. The results showed that the administration of CHBP during cold preservation of kidneys as well as autologous blood could ameliorate IR injury after hemoperfusion, which was associated with increased renal blood supply and improved renal tubular structure and function [65].
\nAs the professional antigen-presenting cells, dendritic cells (DCs) play a triggering role in acute rejection (AR) after transplant surgery. Thus, we investigated the effects of CHBP on DCs in the kidney transplantation model from Lewis to Wistar rats [66]. The results showed that five successive doses of CHBP administration after kidney transplantation could significantly ameliorate AR with the association of lower histological injury, apoptosis, and CD4+ and CD8+ T-cell infiltration in renal allografts. CHBP also reduced the expression of IFN-γ and IL-1β but increased the expression of IL-4 and IL-10 in the serum of receipt. The number of mature DCs was significantly decreased in renal allografts treated with CHBP [66]. Also, the incubation of DCs with CHBP in vitro led to a reduction in TNF-α, IFN-γ, IL-1β and IL-12 levels and an increase of IL-10 level at the protein level in the supernatant [66]. In the mechanism study, CHBP inhibited TLR activation-induced DC maturation by increasing SOCS1 expression through Jak-2/STAT3 signaling [66]. Our study suggested that CHBP suppressed renal allograft AR by inhibiting the maturation of DCs via Jak-2/STAT3/SOCS1 signaling.
\nMesenchymal stem cell (MSC) is a pluripotent stem cell originating from the mesoderm and has the potential to differentiate into multiple types of cells and tissues [67, 68]. Thus, MSC has long been considered as an ideal cell-based therapy in the repairing of tissue injuries. After adoptive transferred in vivo, however, MSCs may confront a variety of undesirable factors that could decrease their viability and activity [69, 70]. Among them, nutrient starvation is the major obstacle for MSCs within injured tissues. In our study regarding the effect of CHBP on MSCs in vitro, we found that CHBP could significantly improve the cell viability and suppress apoptosis of MSCs in a dose-dependent manner [71]. Starvation resulted in the mitochondrial dysfunction, and the treatment of CHBP could alleviate mitochondrial dysfunction by diminishing the oxidative stress from ROS, restore mitochondrial membrane potential and maintain mitochondrial membrane integrity through the activation of Nrf2/Sirt3/FoxO3a pathway [71]. Moreover, MSCs pretreated with CHBP were more resistant to nutrient starvation [71]. This study suggests that CHBP has the e prospects for sustaining stem cell survival under nutrient-deprived conditions and improving the therapeutic effect of MSC-based treatment.
\nThe research about CHBP in our center also includes its effects on other kinds of injuries, for example, aristolochic acid-induced acute kidney injury [72]. The study on the role of CHBP in acute and chronic allograft rejection is in progress as well. Although our understanding about CHBP has significantly increased, there is still plenty of work to do to translate this protective peptide into clinical practice. For example, the pharmacokinetics and pharmacodynamics of CHBP are not examined so far. The dosage form design of this new drug should be improved for oral administration or intravenous injection. The clinical trials are indispensable before it is finally applied for clinical use. In a further study, we plan to investigate the effects of CHBP in primate models of acute organ injury which could better represent the analogous disorders in the human being. We believe that this smaller but stronger peptide derivative of EPO could facilitate the treatment of acute tissue injury shortly.
\nThis study was supported by National Natural Science Foundation of China (grants 81400752; 81770746 to CY).
\nThe authors declare no conflict of interest.
Biogenic amines found in animals, plants, microorganisms, and humans are formed by the decarboxylation of amino acids or amination and transamination of aldehydes and ketones during the standard metabolic processes.
\nBiogenic amines, having several critical biological roles in the body, have essential physiological functions such as the regulation of growth and blood pressure and control of the nerve conduction. Besides, they are required in the immunologic system of intestines and in maintaining the activity of the standard metabolic functions, and when taking the nourishment in high concentrations, they cause disorders in nervous, respiratory, and cardiovascular systems and allergic reactions as well. In this chapter, biosynthesis of biogenic amines, their toxic effects as well as their physiological functions, and their effect on health will be presented.
\nCO2 and biogenic amine occur as a result of the enzymatic reaction catalyzed by pyridoxal phosphate to decarboxylate the amino acid (Figure 1) [1]. Biogenic amines are biologically active molecules, as they are formed by decarboxylation of amino acids or amination and transamination of aldehydes and ketones during standard metabolic processes [2]. Biogenic amines take charge of the proliferation and differentiation of cells and their metabolism by entering into the structure of hormones, cobalamin (vitamin and aminoacetone), and coenzyme A in the body [3]. They have importance regarding the environment by causing water pollution, as their formations pertain to the amino acid and microorganisms [3, 4]. Biogenic amines may cause intoxications when taken in high amounts [5].
\nDecarboxylation of amino acids.
Biogenic amines are organic nitrogen compounds having a low molecular weight [5, 6]. Their chemical structure can be classified as (i) aromatic and heterocyclic (histamine, tryptamine, tyramine, phenylethylamine, and serotonin); (ii) aliphatic di-, tri-, and polyamines (putrescine, cadaverine, spermine, spermidine, and agmatine); and (iii) aliphatic volatile amines (ethylamine, methylamine, isopentylamine, and ethanolamine) (Figure 2) [7, 8]. Besides, their amine group classifications include (i) monoamine (phenylethylamine, tyramine, methylamine, ethylamine, isopentylamine, and ethanolamine), (ii) diamine (histamine, tryptamine, serotonin, putrescine, and cadaverine), and (iii) polyamine (spermine, spermidine, and agmatine) [7, 8, 9].
\nClassification of biogenic amines according to their chemical structures.
Biogenic amines generally occur as a result of free amino acid decarboxylations with the microbial enzymes. Amino acid decarboxylation happens by removal of the α-carboxyl group [10]. Their occurrences are as below: histamine from histidine amino acid, tyramine from tyrosine amino acid, tryptamine and serotonin from tryptophan amino acid, phenylethylamine from phenylalanine amino acid, putrescine from ornithine amino acid, cadaverine from lysine amino acid, and agmatine from arginine amino acid (Figure 3) [11, 12, 13].
\nFormation mechanism of biogenic amines.
Biogenic amines play an essential role in cell membrane stabilization, immune functions, and prevention of chronic diseases, as they participate in the nucleic acid and protein synthesis [14]. Besides, they are compounds created as the growth regulation (spermine, spermidine, and cadaverine), neural transmission (serotonin), and inflammation mediators (histamine and tyramine) [6, 15].
\nHistamine, a standard component of the body, consists of histidine amino acid as a result of histidine decarboxylase activity depending on pyridoxal phosphate (Figure 3) [16]. Histamine distribution and concentration found in the tissues of all vertebrates are very unsteady [17, 18]. Histamine takes charge of some functions related to balancing the body temperature and regulating the stomach volume, stomach pH, and cerebral activities [19] as it participates in the essential functions such as neurotransmission and vascular permeability [20, 21]. However, it also plays a role in starting the allergic reactions [22, 23].
\nTryptamine consists of tryptophan amino acid as a result of the aromatic L-amino acid decarboxylase activity (Figure 3) [24, 25]. Tryptamine is a monoamine alkaloid found in plants, fungi, and animals [26]. Tryptamine, found in trace amounts in mammalian brains, increases blood pressure [10, 27] as well as plays a role as a neurotransmitter or neuromodulator [26].
\nThe amino acid of phenylalanine synthesizes phenylethylamine through the aromatic L-amino acid decarboxylase in humans, some fungi, and bacteria as well as several plants and animal species (Figure 3) [28, 29, 30]. It functions as a neurotransmitter in the human central nervous system [31, 32].
\nTyramine, consisting of tyrosine amino acid as a result of tyrosine decarboxylase activity, is generally found in low amounts (Figure 3) [33, 34, 35, 36]. Tyramine leads to several physiological reactions such as blood pressure increase, vasoconstriction [37], tyramine active noradrenalin secretion, etc., as the sympathetic nervous system controls several functions of the body [38, 39]. Tyramine, stored in the neurons, causes the increase in the tear, salivation and respiratory as well as mydriasis [39].
\nTryptophan synthesizes serotonin as a result of tryptophan hydroxylase and aromatic L-amino acid decarboxylase enzyme activities (Figure 3) [11, 40]. Serotonin, one of the crucial neurotransmitters of the central nervous system, plays a role in plenty of critical physiological mechanisms such as sleep, mood disorders, appetite regulation, sexual behavior, cerebral blood flow regulation, and blood-brain barrier permeability [41, 42].
\nPutrescine consists of ornithine amino acid as a result of ornithine decarboxylase activity. Besides, it may be synthesized by arginine through the agmatine and carbamoylputrescine (Figure 3) [12, 39, 43, 44]. Putrescine, produced by bacteria and fungi, contributes to the cell growth, cell division, and tumorigenesis [45, 46] as it is the preliminary substance of spermidine and spermine [12, 47].
\nCadaverine, synthesized by lysine as a result of lysine decarboxylase enzyme activity, takes charge of the diamine and polyamine formations (Figure 3) [45, 48, 49].
\nSpermidine synthase catalyzes spermidine formation from putrescine (Figure 3) [50, 51]. Spermidine is a precursor of other polyamines such as spermine and structural isomer thermospermine [45, 52]. Spermidine, regulating several crucial biological processes (Na+-K+ ATPaz), protects the membrane potential and controls the intracellular pH and volume [53]. Besides, spermidine, a polyamine found in the cellular metabolism, has a role in the neuronal nitric oxide synthase inhibitions and intestinal tissue developments [54].
\nSpermine, whose precursor amino acid is ornithine, is formed from spermidine through the spermine synthase enzyme (Figure 3) [51]. Spermine is present in several organisms and tissues, as it is a polyamine that is found in all eukaryotic cells and has a role in the cellular metabolism [52, 55]. It plays a role in the intestinal tissue developments and stabilizes the helical structure in viruses [52, 56, 57].
\nAgmatine is a biogenic amine formed by arginine decarboxylase enzyme activity of arginine amino acid (Figure 3) [12, 44, 58]. Agmatine participates in the polyamine metabolism over the putrescine hydrolyzed by the agmatine enzyme and has several functions such as nitric oxide synthesis regulation, polyamine metabolism, and matrix metalloproteinase and enzyme activity leading to H2O2 production [59, 60].
\nThe detoxification system, splitting the biogenic amines in the human body, consists of monoamine oxidase (MAO), diamine oxidase (DAO), polyamine oxidase (PAO), and histamine-N-methyl transferase (HNMT) [17, 61, 62].
\nBiogenic amines have several important biological roles in the body and constitute the first step of protein, hormone, and nucleic acid synthesis [61, 63]. The polyamines such as putrescine, spermine, and spermidine are the unique components of living cells. Besides, the polyamines were stated to require maintaining the intestinal immunologic systems and healthy metabolic function activities [52, 64, 65, 66, 67]. The biogenic amines cause respiratory disorders, headache, tachycardia, hypo- or hypertension, and allergic reactions when taken in high concentrations together with nutrients [68].
\nBiogenic amines are vasoactive components, and taking them in high amounts leads to change in blood pressure in humans and animals. The amines bear essential psychoactive or vasoactive effects, as they have the biological activities such as histamine, tryptamine, tyramine, and phenylethylamine [33]. Histamine is a biologically active amine and quickly scatters to the tissues through blood circulation and leads to several reactions. However, in the case where aminoxidase enzyme inhibitors are present in the environment, the biogenic amine prevents detoxification, and health problems (erythema, edema, rash, headache, burning, etc.) show up [17, 68]. Histamine also has essential metabolic functions such as a role in the nervous system functions and blood pressure control. It mainly takes effect by binding to the cardiovascular system (vasodilatation and hypotension) and cell membrane receptors in several secretory glands (such as gastric acid secretion) [22, 23]. In addition to them, it may lead to some neurotransmission disorders and causes headache, flushing, gastrointestinal disorders, and edema by giving rise to blood vessel dilatations [61, 69]. Histamine intoxicates when orally taken in amounts of 8 mg and above [3]. Individuals generally have lower intestinal oxidase enzyme activities according to the healthy persons, as they hold the gastrointestinal problems such as gastritis, stomach and colonic ulcers [6, 69].
\nIntestinal mucosal injuries may decrease the enzyme functions by detoxifying the biogenic amines [17, 63]. The DAO activity disruption causes histamine intolerance and also allergic reactions as a result of the drug utilization, as it is caused by genetic and gastrointestinal diseases or DAO inhibition [17, 70]. It was found to increase the histamine toxicity by preventing the histamine oxidation of putrescine, cadaverine, and agmatine in humans [71].
\nBiogenic amines lead to hypertension, as they have vasoconstriction effects such as tyramine, phenylethylamine, and tryptamine [37, 68, 72]. Consuming tyramine-rich nutriments was found to react with the tyramine MAO inhibitor drugs and cause hypertensive crisis and also migraine in some patients [73]. Tyramine is revealed to inhibit MAO, tryptamine DAO, phenylethylamine DAO, and HNMT enzymes [74, 75].
\nIn the case of deficiency of putrescine, found in the high concentration in brains, is stated to develop the depression and also useful in the depression physiopathology [3, 76].
\nThe pharmacological effects of putrescine, cadaverine, spermine, and spermidine are at lower levels according to histamine, tyramine, and phenylethylamine [77]. Putrescine, causing hypotension, bradycardia, and lockjaw, creates carcinogenic heterocyclic compounds including nitrosamine, nitrosopyrrolidine, and nitrosopiperidine as some biogenic amines such as cadaverine, spermine, and spermidine react with the nitrite [5, 10, 39, 78].
\nPolyamines are known to lead to low-dose colon cancer by affecting the cell developments and differentiation [79, 80]. In addition to them, putrescine, cadaverine, spermine, and spermidine were also found to induce apoptosis and inhibit cell proliferation. The high-dose putrescine was found to induce apoptosis and prevent the spread [81, 82]. This putrescine effect pertains to increasing the nitric oxide synthesis, inhibiting the redox reactions and binding directly to the carcinogenic agents [82].
\nEating disorders such as anorexia nervosa and bulimia nervosa disrupt the function of brain serotonin [83]. Albumin deficiency shows up due to inadequate nutrition, and tryptophan transition from the blood-brain barrier increases, as it could not connect to the albumin. As a consequence, an increase occurs in the brain serotonin concentration [84, 85]. The drugs (MAO inhibitors) are used, as they change the serotonin levels in the depression, generalized anxiety disorder, and social phobia treatments [86]. The MAO inhibitors, used in treating these diseases, increase the brain concentrations by preventing the neurotransmitter (serotonin) disruptions [73, 86].
\nAgmatine shows a nephroprotective effect by increasing the glomerular filtration rate, and it also has a hypoglycemic impact as a result of several molecular mechanisms taking place in the blood glucose regulation [56, 87]. Besides, the agmatine level of schizophrenia patients was shown to be higher compared to that of healthy humans [88].
\nThe present information related to biogenic amines having different physiological functions and similar chemical structures and metabolic pathways was updated, undesirable effects were considered more comprehensively for human and animal health, and information was submitted about the essential diseases caused by biogenic amines.
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\n\nOut of all of the publishing options available to researchers, why choose to contribute your research to an IntechOpen Edited Volume? The reasons are simple. IntechOpen has worked exceptionally hard over the past years to fine tune the Open Access book publishing process and we continue to work hard to deliver the best for all of our contributors. The quality of published content is of utmost importance to us, followed closely by speed, and of course, availability and accessibility. To view current Open Access book projects that are Open for Submissions visit us here.
\n\nQUALITY CONTENT
\n\nOver the years we have learned what is important. What makes a difference to the researchers that work with us, what they value. Something that is very high not only on their lists, but our own, is the quality of the published content.
\n\nOur books contain scientific content written by two Nobel Prize winners, two Breakthrough Prize winners and 73 authors who are in the top 1% Most Cited.
\n\nWith regular submission for coverage in the single most important database, the Book Citation Index in the Web of Science™ Core Collection (BKCI), and no rejected submissions to date, over 43% of all Open Access books indexed in the BKCI are IntechOpen published books.
\n\nIn addition to BKCI, IntechOpen covers a number of important discipline specific databases as well, such as Thomson Reuters’ BIOSIS Previews.
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\n\nThe need for up to date information available at the click of a mouse is one thing that sets IntechOpen apart. By developing our own technologies in order to streamline the publishing process, we are able to minimize the amount of time from initial submission of a manuscript to its final publication date, without compromising the rigor of the editorial and peer review process. This means that the research published stays relevant, and in this fast paced world, this is very important.
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\n\nThe utilization of CC licenses allow researchers to retain copyright to their work. Researchers are free to use, adapt and share all content they publish with us. You will never have to pay permission fees to reuse a part of an experiment that you worked so hard to complete and are free to build upon your own research and the research of others. The Edited Volume helps bring together research from all over the world and compiles that research into one book - accessible for all. The research presented in chapter one can inspire the author of chapter three to take his or her research to the next level. It is about sharing ideas, insights and knowledge.
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\n\nOur Open Access book collection includes:
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I received a B.Eng. degree in Computer Engineering with First Class Honors in 2008 from Prince of Songkla University, Songkhla, Thailand, where I received a Ph.D. degree in Electrical Engineering. My research interests are primarily in the area of biomedical signal processing and classification notably EMG (electromyography signal), EOG (electrooculography signal), and EEG (electroencephalography signal), image analysis notably breast cancer analysis and optical coherence tomography, and rehabilitation engineering. I became a student member of IEEE in 2008. During October 2011-March 2012, I had worked at School of Computer Science and Electronic Engineering, University of Essex, Colchester, Essex, United Kingdom. In addition, during a B.Eng. I had been a visiting research student at Faculty of Computer Science, University of Murcia, Murcia, Spain for three months.\n\nI have published over 40 papers during 5 years in refereed journals, books, and conference proceedings in the areas of electro-physiological signals processing and classification, notably EMG and EOG signals, fractal analysis, wavelet analysis, texture analysis, feature extraction and machine learning algorithms, and assistive and rehabilitative devices. I have several computer programming language certificates, i.e. Sun Certified Programmer for the Java 2 Platform 1.4 (SCJP), Microsoft Certified Professional Developer, Web Developer (MCPD), Microsoft Certified Technology Specialist, .NET Framework 2.0 Web (MCTS). 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