\\n\\n
IntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
\\n\\nBy listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
\\n\\nAll three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
\\n\\n"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
\\n\\n"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
\\n\\nIn conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\\n\\n“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\\n\\nWe invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\\n\\nFeel free to share this news on social media and help us mark this memorable moment!
\\n\\n\\n"}]',published:!0,mainMedia:{caption:"",originalUrl:"/media/original/237"}},components:[{type:"htmlEditorComponent",content:'
After years of being acknowledged as the world's leading publisher of Open Access books, today, we are proud to announce we’ve successfully launched a portfolio of Open Science journals covering rapidly expanding areas of interdisciplinary research.
\n\n\n\nIntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
\n\nBy listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
\n\nAll three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
\n\n"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
\n\n"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
\n\nIn conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\n\n“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\n\nWe invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\n\nFeel free to share this news on social media and help us mark this memorable moment!
\n\n\n'}],latestNews:[{slug:"webinar-introduction-to-open-science-wednesday-18-may-1-pm-cest-20220518",title:"Webinar: Introduction to Open Science | Wednesday 18 May, 1 PM CEST"},{slug:"step-in-the-right-direction-intechopen-launches-a-portfolio-of-open-science-journals-20220414",title:"Step in the Right Direction: IntechOpen Launches a Portfolio of Open Science Journals"},{slug:"let-s-meet-at-london-book-fair-5-7-april-2022-olympia-london-20220321",title:"Let’s meet at London Book Fair, 5-7 April 2022, Olympia London"},{slug:"50-books-published-as-part-of-intechopen-and-knowledge-unlatched-ku-collaboration-20220316",title:"50 Books published as part of IntechOpen and Knowledge Unlatched (KU) Collaboration"},{slug:"intechopen-joins-the-united-nations-sustainable-development-goals-publishers-compact-20221702",title:"IntechOpen joins the United Nations Sustainable Development Goals Publishers Compact"},{slug:"intechopen-signs-exclusive-representation-agreement-with-lsr-libros-servicios-y-representaciones-s-a-de-c-v-20211123",title:"IntechOpen Signs Exclusive Representation Agreement with LSR Libros Servicios y Representaciones S.A. de C.V"},{slug:"intechopen-expands-partnership-with-research4life-20211110",title:"IntechOpen Expands Partnership with Research4Life"},{slug:"introducing-intechopen-book-series-a-new-publishing-format-for-oa-books-20210915",title:"Introducing IntechOpen Book Series - A New Publishing Format for OA Books"}]},book:{item:{type:"book",id:"6925",leadTitle:null,fullTitle:"Endoplasmic Reticulum",title:"Endoplasmic Reticulum",subtitle:null,reviewType:"peer-reviewed",abstract:"The purpose of this book is to concentrate on recent developments on endoplasmic reticulum. The articles collected in this book are contributions by invited researchers with a long-standing experience in different research areas. We hope that the material presented here is understandable to a broad audience, not only scientists but also people with general background in many different biological sciences. This volume offers you up-to-date, expert reviews of the fast-moving field of endoplasmic reticulum. The book is divided in two sections: 1. Introduction and 2. Endoplasmic Reticulum Properties and Functions.",isbn:"978-1-83880-088-8",printIsbn:"978-1-83880-087-1",pdfIsbn:"978-1-83962-136-9",doi:"10.5772/intechopen.73456",price:119,priceEur:129,priceUsd:155,slug:"endoplasmic-reticulum",numberOfPages:106,isOpenForSubmission:!1,isInWos:null,isInBkci:!1,hash:"a9e90d2dbdbc46128dfe7dac9f87c6b4",bookSignature:"Angel Català",publishedDate:"April 17th 2019",coverURL:"https://cdn.intechopen.com/books/images_new/6925.jpg",numberOfDownloads:6982,numberOfWosCitations:7,numberOfCrossrefCitations:7,numberOfCrossrefCitationsByBook:0,numberOfDimensionsCitations:16,numberOfDimensionsCitationsByBook:0,hasAltmetrics:1,numberOfTotalCitations:30,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 28th 2018",dateEndSecondStepPublish:"August 13th 2018",dateEndThirdStepPublish:"October 12th 2018",dateEndFourthStepPublish:"December 31st 2018",dateEndFifthStepPublish:"March 1st 2019",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"196544",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",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",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"5",totalChapterViews:"0",totalEditedBooks:"6",institution:{name:"National University of La Plata",institutionURL:null,country:{name:"Argentina"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"47",title:"Cell Biology",slug:"biochemistry-genetics-and-molecular-biology-cell-biology"}],chapters:[{id:"64426",title:"Introductory Chapter: Endoplasmic Reticulum-Knowledge and Perspectives",doi:"10.5772/intechopen.82089",slug:"introductory-chapter-endoplasmic-reticulum-knowledge-and-perspectives",totalDownloads:931,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:null,signatures:"Angel Catala",downloadPdfUrl:"/chapter/pdf-download/64426",previewPdfUrl:"/chapter/pdf-preview/64426",authors:[{id:"196544",title:"Prof.",name:"Angel",surname:"Catala",slug:"angel-catala",fullName:"Angel Catala"}],corrections:null},{id:"64634",title:"Mechanical Properties of Chaperone BiP, the Master Regulator of the Endoplasmic Reticulum",doi:"10.5772/intechopen.82080",slug:"mechanical-properties-of-chaperone-bip-the-master-regulator-of-the-endoplasmic-reticulum",totalDownloads:1178,totalCrossrefCites:2,totalDimensionsCites:3,hasAltmetrics:0,abstract:"Immunoglobulin heavy-chain-binding protein (BiP protein) is a 75-kDa Hsp70 monomeric ATPase motor that plays broad and crucial roles maintaining proteostasis inside the cell. Its malfunction has been related with the appearance of many and important health problems such as neurodegenerative diseases, cancer, and heart diseases, among others. In particular, it is involved in many endoplasmic reticulum (ER) processes and functions, such as protein synthesis, folding, and assembly, and also it works in the posttranslational mechanism of protein translocation. However, it is unknown what kind of molecular motor BiP works like, since the mechanochemical mechanism that BiP utilizes to perform its work during posttranslational translocation across the ER is not fully understood. One novel approach to study both structural and catalytic properties of BiP considers that the viscoelastic regime behavior of the enzymes (considering them as a spring) and their mechanical properties are correlated with catalysis and ligand binding. Structurally, BiP is formed by two domains, and to establish a correlation between BiP structure and catalysis and how its conformational and viscoelastic changes are coupled to ligand binding, catalysis, and allosterism (information transmitted between the domains), optical tweezers and nano-rheology techniques have been essential in this regard.",signatures:"Hilda M. Alfaro-Valdés, Francesca Burgos-Bravo, Nathalie Casanova-Morales,\nDiego Quiroga-Roger and Christian A.M. Wilson",downloadPdfUrl:"/chapter/pdf-download/64634",previewPdfUrl:"/chapter/pdf-preview/64634",authors:[{id:"270726",title:"Prof.",name:"Christian A.M.",surname:"Wilson",slug:"christian-a.m.-wilson",fullName:"Christian A.M. Wilson"},{id:"270727",title:"MSc.",name:"Hilda M.",surname:"Alfaro-Valdes",slug:"hilda-m.-alfaro-valdes",fullName:"Hilda M. Alfaro-Valdes"},{id:"270728",title:"Dr.",name:"Francesca",surname:"Burgos-Bravo",slug:"francesca-burgos-bravo",fullName:"Francesca Burgos-Bravo"},{id:"270729",title:"Dr.",name:"Diego",surname:"Quiroga-Roger",slug:"diego-quiroga-roger",fullName:"Diego Quiroga-Roger"},{id:"270730",title:"Dr.",name:"Nathalie",surname:"Casanova-Morales",slug:"nathalie-casanova-morales",fullName:"Nathalie Casanova-Morales"}],corrections:null},{id:"65506",title:"Endoplasmic Reticulum-Associated Degradation (ERAD)",doi:"10.5772/intechopen.82043",slug:"endoplasmic-reticulum-associated-degradation-erad-",totalDownloads:1759,totalCrossrefCites:2,totalDimensionsCites:2,hasAltmetrics:0,abstract:"The newly synthesized proteins are kept in the endoplasmic reticulum (ER) until their maturation is completed. The accurate protein folding is vital for homeostasis, but this process is error-prone since it is chemically complicated. Aberrant folding may result in aggregates having a toxic gain of function or may lead to a loss of protein function; therefore, protein misfolding can lead to several pathologies. The ER protein quality control mechanism monitors the fidelity of protein folding. Those proteins that fail to fold or assemble properly are subjected to degradation via a process known as ER-associated degradation (ERAD). Besides clearing proteins having folding problems, ERAD is also known to regulate the levels of some physiological proteins including 3-hydroxy-3-methylglutaryl-coenzymeA reductase (HMGR) catalyzing the rate-limiting step of cholesterol biosynthesis. ERAD is a complex, multistep process starting with the recognition and targeting of substrates, followed by ubiquitination, retrotranslocation and proteasomal degradation. A large number of ERAD factors functioning in different molecular machineries increases the complexity of mammalian ERAD. ERAD is fundamental for human health and there is increasing evidence linking ERAD with various diseases. Here, the different modules/machineries of the ERAD process together with its tight regulation will be discussed.",signatures:"Burcu Erbaykent Tepedelen and Petek Ballar Kirmizibayrak",downloadPdfUrl:"/chapter/pdf-download/65506",previewPdfUrl:"/chapter/pdf-preview/65506",authors:[{id:"263603",title:"Prof.",name:"Petek",surname:"Ballar",slug:"petek-ballar",fullName:"Petek Ballar"},{id:"280728",title:"Dr.",name:"Burcu",surname:"Erbaykent Tepedelen",slug:"burcu-erbaykent-tepedelen",fullName:"Burcu Erbaykent Tepedelen"}],corrections:null},{id:"64217",title:"Endoplasmic Reticulum Stress and Autophagy",doi:"10.5772/intechopen.81381",slug:"endoplasmic-reticulum-stress-and-autophagy",totalDownloads:2076,totalCrossrefCites:1,totalDimensionsCites:9,hasAltmetrics:1,abstract:"In eukaryotic cells, the aggregation of the endoplasmic reticulum (ER)-mediated unfolded or misfolded proteins leads to disruption of the ER homeostasis, which can trigger ER stress. To restore the ER homeostasis, the ER stress activates the intracellular signaling cascade from the ER to the nucleus, referred to as the unfolded protein response (UPR). Autophagy primitively portrayed as an evolutionarily conserved process is involved in cellular homeostasis by facilitating the lysosomal degradation pathway for the recycling and elimination of intracellular defective macromolecules and organelles. Autophagy is tightly regulated by the protective mechanism of UPR. The UPR and autophagy are interlinked, which indicates that the ER stress can not only induce autophagy but also suppress it. Here, we discuss the molecular mechanism of ER stress and autophagy and their induction and inhibition signaling network.",signatures:"Mohammad Fazlul Kabir, Hyung-Ryong Kim and Han-Jung Chae",downloadPdfUrl:"/chapter/pdf-download/64217",previewPdfUrl:"/chapter/pdf-preview/64217",authors:[{id:"264625",title:"Prof.",name:"Han-Jung",surname:"Chae",slug:"han-jung-chae",fullName:"Han-Jung Chae"},{id:"264666",title:"Prof.",name:"Hyung-Ryong",surname:"Kim",slug:"hyung-ryong-kim",fullName:"Hyung-Ryong Kim"},{id:"271187",title:"Mr.",name:"Mohammad Fazlul",surname:"Kabir",slug:"mohammad-fazlul-kabir",fullName:"Mohammad Fazlul Kabir"}],corrections:null},{id:"65680",title:"Endoplasmic Reticulum Stress during Mammalian Follicular Atresia",doi:"10.5772/intechopen.82687",slug:"endoplasmic-reticulum-stress-during-mammalian-follicular-atresia",totalDownloads:1041,totalCrossrefCites:2,totalDimensionsCites:2,hasAltmetrics:0,abstract:"Follicles are ovarian structures that contain a single germ cell. During the mammalian reproductive lifetime, ovarian follicles mature through the process of follicular development, with the aim of selecting oocytes for ovulation. As part of this process, several follicles are eliminated by means of follicular atresia, a mechanism that mainly involves apoptosis. Nevertheless, it has been shown that there are other routes of programmed cell death in the ovary including autophagy, paraptosis, and necroptosis. Surprisingly, the endoplasmic reticulum is involved in these different programmed cell death pathways. Moreover, there are several evidences for the pathways triggered by intra- and extracellular signals in endoplasmic reticulum-induced cell death. Thus, it is important to analyze the participation of endoplasmic reticulum in follicular atresia.",signatures:"Nayeli Torres-Ramírez, Rosario Ortiz-Hernández, M. Luisa Escobar-Sánchez,\nOlga M. Echeverría-Martínez and Gerardo H. Vázquez-Nin",downloadPdfUrl:"/chapter/pdf-download/65680",previewPdfUrl:"/chapter/pdf-preview/65680",authors:[{id:"163923",title:"Prof.",name:"Gerardo Hebert",surname:"Vázquez-Nin",slug:"gerardo-hebert-vazquez-nin",fullName:"Gerardo Hebert Vázquez-Nin"},{id:"175255",title:"Dr.",name:"Ml",surname:"Escobar",slug:"ml-escobar",fullName:"Ml Escobar"},{id:"175256",title:"Dr.",name:"Echeverría",surname:"Om",slug:"echeverria-om",fullName:"Echeverría Om"},{id:"278117",title:"Dr.",name:"Nayeli",surname:"Torres-Ramírez",slug:"nayeli-torres-ramirez",fullName:"Nayeli Torres-Ramírez"},{id:"284930",title:"Dr.",name:"Rosario",surname:"Ortíz-Hernández",slug:"rosario-ortiz-hernandez",fullName:"Rosario Ortíz-Hernández"}],corrections:null}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},subseries:{id:"11",series:{id:"10",title:"Physiology",issn:"2631-8261",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,position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"2",totalChapterViews:"0",totalEditedBooks:"1",institution:{name:"Jagiellonian University",institutionURL:null,country:{name:"Poland"}}}}},tags:null},relatedBooks:[{type:"book",id:"2553",title:"Lipid Peroxidation",subtitle:null,isOpenForSubmission:!1,hash:"b39734aa940b2d63ae5e8773d3dd5280",slug:"lipid-peroxidation",bookSignature:"Angel Catala",coverURL:"https://cdn.intechopen.com/books/images_new/2553.jpg",editedByType:"Edited by",editors:[{id:"196544",title:"Prof.",name:"Angel",surname:"Catala",slug:"angel-catala",fullName:"Angel 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\r\n\t1. Emphasizing the unique power of the molecular docking method in new drug discovery;
\r\n\t2. Demonstration of how the molecular docking technique has led to the discovery of new molecules in cancer therapy, proteasome, and STAT3 inhibition, and the treatment of Alzheimer's disease;
\r\n\t3. Underlining the importance of molecular docking-based modeling methods in the various branches of biotechnology
\r\n\tWe hope that this book will be a common point where researchers working in the fields of life sciences and drug development will eventually meet.
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Drăgoi"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},onlineFirst:{chapter:{type:"chapter",id:"81796",title:"Apoptosis-Related Diseases and Peroxisomes",doi:"10.5772/intechopen.105052",slug:"apoptosis-related-diseases-and-peroxisomes",body:'Death is the final fate of cells and organisms and is a normal biological phenomenon in the living world. Cell death plays a crucial role in the development of plants and animals in nature and in maintaining ecological balance [1]. For example, in the developing vertebrate nervous system, as many as half or more of the nerve cells usually die soon after they are formed. In a healthy adult human, billions of cells die every hour in the bone marrow and intestines. So much cell death seems very wasteful, especially when the vast majority of cells are perfectly healthy at the time of suicide.
In general, cell death can be divided into two types: programmed cell death (PCD) and accidental cell death (necrosis) [2]. The former is a controlled process of intracellular death program, also vividly referred to as cellular suicide. The latter is caused by external factors (i.e., injury, infection, etc.). The study of PCD (especially apoptosis) processes has led to a better understanding of the pathogenesis of certain diseases. The 2002 Nobel Prize in Physiology and Medicine was awarded to Britons Sydney Brenner, Jone E. Sulston, and H Robert Horvitz for their discovery of how genes regulate organ growth and programmed cell suicide processes, using the nematode
A coordinated balance between cell proliferation and apoptosis is crucial for normal development and tissue homeostasis. Once this balance is permanently disrupted, normal cells may be transformed into mutant cells whose clonal survival and uncontrolled proliferation may lead to the development of tumors and various other diseases.
Apoptosis is the process of cellular suicide by activating an intracellular death program or by the orderly breakdown of cells from within. The term was first introduced by Kerr J. F. R. in the 1970s and was not accepted by the general public until the 1990s.
Although apoptosis is only one form of Programmed cell death (PCD), it is by far the most common and well-understood form, and, confusingly, biologists often use the terms PCD and apoptosis interchangeably [3].
For a multicellular organism, a highly organized community, cell numbers are tightly regulated not only by controlling the rate of cell division but also by controlling the rate of cell death. Thus, apoptosis is important not only for tissue remodeling and elimination of transitional organs during the development of an organism, but also for the clearance of cellular senescence inactive metabolic organs, such as blood cells and epithelial cells in the digestive system, and cells with damaged or mutated DNA [4, 5, 6]. In a nutshell, apoptosis is an essential mechanism complementary to proliferation to ensure homeostasis in all tissues.
Unlike apoptosis, necrosis is a form of cell injury that leads to the premature death of cells in living tissues due to autolysis, usually caused by stronger external factors such as infection, toxins, or trauma, ultimately resulting in the unregulated of cellular components, always harmful and potentially fatal to the organism [7, 8]. Necrosis usually causes a local inflammatory response. The reason for this is that when nearby macrophages engulf these necrotic cells, they may release microorganisms that destroy the surrounding tissue causing collateral damage and inhibiting the healing process.
Typically, cell death due to necrosis does not follow the apoptotic signaling transduction pathway, but rather various receptors are activated, leading to loss of cell membrane integrity and uncontrolled release of cell death products into the extracellular space. In contrast, apoptosis is a naturally occurring programmed and targeted cause of cell death and usually provides beneficial effects to the organism. A brief comparison of them can be summarized as follows (Figure 1).
Structural change of cells undergoing necrosis and apoptosis.
As mentioned above, necrosis is a form of traumatic cell death caused by acute cellular injury. In contrast, apoptosis is a process of active cellular suicide. Multicellular organisms eliminate mutated, damaged, or unwanted cells by this type of active suicide. Apoptosis plays an important role in tissue sculpting during embryonic development and in the maintenance of tissue homeostasis throughout life [6].
The process has distinct morphological features, including cell rounding and contraction, blebbing and PS externalization of the plasma membrane, cytoplasmic vacuolization including endoplasmic reticulum expansion and cisternae swelling to form vesicles and vacuoles, nuclear condensation, border aggregation or fragmentation, chromatin compaction, pyknosis, and ultimately fragmentation between nucleosomes by endonucleases, resulting in regular DNA degradation and inhibition of protein translation, and ultimately to the eventual rupture of the cell into small spheres surrounded by membranes called apoptotic bodies, which contain “packed” cell contents with an electron cloud density similar to chromatin; and a sub-G1 curve preceding the G1 phase peak is observed in cytometric histogram [9]. Apoptotic bodies can be recognized and digested by phagocytosis of neighboring macrophages through the presence of phosphatidylserine (PS) on their surface [10]. In this way, the apoptotic cells can be rapidly removed by tissue phagocytes through phagocytosis, without releasing harmful substances that can initiate inflammation, which can cause a significant amount of tissue damage. Because apoptotic cells are always rapidly eaten and digested, dead cells are usually rarely seen, even when large numbers of cells die from apoptosis. This may be the reason why biologists once ignored the phenomenon of apoptosis and may still underestimate its extent.
Abnormal apoptosis contributes to many important diseases, including cancer, autoimmune diseases, diabetes, and neurodegenerative diseases. Various types of cellular stress, such as DNA damage or growth factor deprivation, can trigger apoptosis through intrinsic or extrinsic pathways.
Apoptosis can be triggered by both internal stimuli, such as abnormalities in DNA, and external stimuli, such as certain cytokines from different pathways, respectively [11]; or it can be induced by physiological or pathological factors.
Specifically, physiological triggers can include the following two aspects [12]: (1) Direct action of certain hormones and cytokines: for example, glucocorticoids are typical signals of apoptosis in lymphocytes; thyroxine plays an important role in the apoptotic degeneration of tadpoles’ tails; TNF can induce apoptosis in a variety of cells. (2) Indirect effects of certain hormones and cytokines: for example, testosterone deficiency caused by testicular dysplasia can lead to apoptosis of prostate epithelial cells. Inadequate secretion of adrenocorticotropic hormone by the pituitary gland can promote apoptosis of adrenocortical cells, etc.
While pathological triggers usually include the following two aspects: (1) It is generally believed that apoptosis can be induced by many factors that can cause damage to cells, such as stress, radiation, chemical toxins, viral infections, and chemotherapeutic drugs, and even malnutrition and excessive functional complexes can induce apoptosis. (2) Some factors such as various chemical carcinogens and certain viruses (e.g., EBV) inhibit apoptosis. Therefore, it is thought that the ability to induce cells may be related to the type, intensity, and duration of the harmful factors.
The initiation of apoptosis is tightly regulated by different signaling pathways. The best-understood two are the intrinsic pathway (also known as the mitochondrial pathway) and the extrinsic pathway (also known as the death receptor pathway). The mitochondrial pathway is generally activated by intracellular signals and depends on proteins released from the intermembrane space between the mitochondrial bilayers. The death receptor pathway is activated by extracellular ligands, and the activated extracellular ligands bind to their specific death receptors on the cell surface, inducing the formation of death-inducing signaling complexes (DISC) [13, 14]. Here, we will discuss the extrinsic and intrinsic pathways separately. However, it should be noted that there is crosstalk between these pathways and that extracellular apoptotic signaling can also lead to activation of the intrinsic pathway.
The extrinsic death pathway triggers receptor-mediated apoptosis. Its major components include pro-apoptotic ligands, receptors that recognize/bind ligands, and adaptor proteins that bind to the cytoplasmic face of the receptor. In addition, the pathway recruits other molecules, including cysteine-specific proteases (caspases), the initiator of the death process, and the executors, to execute the apoptotic process [15]. For example, TNF is a common pro-apoptotic ligand and TNFR1 on the cell membrane is the receptor. When TNF binds to TNFR1, the activated receptor binds to two different cytoplasmic adaptor proteins (tumor necrosis factor-related death domain protein, TRADD, and fas-associating protein with death domain, FADD) and procaspase-8, forming a multi-protein complex on the inner surface of the plasma membrane, containing an 80 amino acid death structure domain through which a death-inducing signaling complex (DISC). The cytoplasmic structural domains of the TNF receptor, FADD, and TRADD interact through homologous regions called death structural domains present in each protein [16]. Procaspase-8 and FADD interact through homologous regions called death effector domains. Procaspase 8 in DISC is activated and active caspase 8 is released into the cytoplasm, where it cleaves and activates effector caspases (e.g., procaspase 3), triggering a caspase cascade that further cleaves a number of death substrates, including BID and cytoskeletal proteins, if glued, leading to apoptosis (Figure 2). Notably, inhibitors of apoptosis (IAPs) can inactivate caspases by specifically binding to their active sites. Caspase activator (SMAC)/Diablo and its functional homologs in flies, including Grim, Reaper, and Hid, can in turn target binding and degrade IAPs [17].
Schematic diagram of apoptotic signaling.
In addition, it should be noted that the interaction between TNF and TNFR1 may also activate other signaling pathways and allow cell survival rather than self-destruction.
In general, internal stimuli such as irreparable genetic damage, hypoxia (lack of oxygen), very high concentrations of cytosolic Ca2+, viral infection, or severe oxidative stress (i.e., production of large amounts of damaging free radicals) and cytotoxic drug treatment trigger apoptosis via the intrinsic pathway.
The intrinsic death pathway, i.e., the mitochondrial-received apoptotic pathway, is a death receptor non-dependent apoptotic pathway [18]. This pathway is activated by the release of cytochrome C (Cyto C) from mitochondria in response to various stresses and developmental death cues. The process specifically involves multiple steps as follows: apoptotic signals (various types of cellular stress), lead to the insertion of pro-apoptotic members of the Bcl-2 family of proteins (e.g., Bax), into the outer mitochondrial membrane, forming pores that mediate the release of Cyto C from the mitochondrial intermembrane space into the cell membrane. Once in the cell membrane, Cyto C molecules bind to Apaf-1 (a homolog of mammalian CED4) and further recruit procaspase-9 to form a complex of multiple subunits called the apoptosome. Then procaspase-9 is activated to become active caspase-9. Then the caspase-9 molecule cleaves and activates the downstream executor caspase (Caspase-3, 6,7) to carry out the apoptotic process (Figure 2) [19].
Bcl-2, the mammalian homolog of Ced-9, prevents apoptosis by inhibiting the release of CytoC from mitochondria [20]. IAPs, second mitochondrial activators of caspases (Smac), endonuclease G (Endo G), and AIF also have important roles in the apoptotic process [21]. Notably, Endo G and AIF are specifically activated by apoptotic stimuli and are able to induce ribosomal breakage of DNA independently of caspases. Endo G is a mitochondria-specific nuclease that translocates to the nucleus and cleaves chromatin DNA during apoptosis. AIF is a flavin adenine dinucleotide-containing, NADH-dependent oxidoreductase that resides in the mitochondrial intermembrane space, and its specific enzymatic activity remains unknown. In the presence of apoptosis, AIF undergoes proteolysis and translocates to the nucleus, where it triggers chromatin condensation and massive DNA degradation in a caspase-independent manner.
Previously, it was thought that the only apoptotic pathways were the mitochondrial pathway and the death receptor signaling pathway. Now, an increasing number of studies have shown that the endoplasmic reticulum (ER) also senses and transmits apoptotic signals [22, 23]. The sustained action of various apoptosis-inducing factors may induce a complex unfolded protein response (UPR) by interfering with the correct protein folding process. The UPR response causes endoplasmic reticulum stress, leading to cellular apoptosis due to the accumulation of intracellular misfolded proteins. ER, in addition to being the site of protein folding, it is also the main intracellular Ca2+ reservoir. Disturbing intracellular Ca2+ homeostasis can also induce the typical ER stress response. Interestingly, the localization of Bcl-2 family proteins (including Bcl-1, Bax, Bak,
It has been suggested that procaspase-12 is a proximal effector of apoptosis associated with the ER. Recent studies have found that although caspase-12 is processed and activated in ER stress-induced apoptosis in mouse cells, the enzyme is not absolutely necessary for this process. On the other hand, cells lacking caspase-8 or caspase-9 were highly resistant to ER stress-induced apoptosis. One of the mechanisms that could explain caspase-8 activation in the ER involves the recent discovery of an ER-resident potential apoptosis initiator, named neurotrophic receptor-like death domain protein (NRADD). This protein has a transmembrane and cytoplasmic region that is highly homologous to the death receptor. Induction of apoptosis by NRADD is dependent on caspase-8 activation but does not require the mitochondrial component of the death program.
In addition to propagating death-inducing stress signals, ER contributes to apoptosis initiated by cell surface death receptors and to pathways resulting from DNA damage. Modulation of ER calcium stores can sensitize mitochondria to direct pro-apoptotic stimuli and promote activation of cytoplasmic death pathways.
In short, the extrinsic (receptor-mediated), intrinsic (mitochondria-mediated), and endoplasmic reticulum stress-mediated apoptotic pathways ultimately converge by activating the same caspases, which cleave the same cellular targets. Apoptosis-inducing factors can be involved in diseases by activating apoptotic pathways that affect the rate of apoptosis, and may predominantly involve the first two pathways or all three of these pathways.
The mechanism by which apoptosis occurs is highly conserved in all animal cells. It is dependent on a family of proteins called caspases (c for cysteine and asp for aspartic acid). This family of proteins has many members and generally exists as inactive precursors (procaspases). Procaspases are generally activated by the catalytic cleavage of other (already active) caspases, forming an amplified network of protein cascades. The activation process of procaspases involves the formation of a heterodimer by cleavage and the combination of two dimers to form an active tetramer. During apoptosis, those responsible for initiation are known as initiator caspases; those responsible for cleavage of specific target proteins (e.g. nuclear lamina proteins, DNA degradation enzymes, cytoskeletal proteins, and cell–cell adhesion proteins) are the executor caspases.
Apoptotic mechanisms are present throughout the initial to final stages of animal development. Only the process requires a trigger to be activated for its occurrence. So, how is the first member of the caspase cascade reaction described above initiated? Initiator procaspases usually contain a caspase recruitment domain (CARD). This structural domain can assemble into an activation complex with an adaptor protein when the cell receives an apoptotic signal. The formation of this complex means that the promoter caspase will be activated by cleavage.
As mentioned above, there are numerous members of the caspases family, most of which are involved in apoptosis, but not all of them mediate apoptosis [24]. For example, the first discovered caspase, human interleukin-l-converting enzyme (ICE), was not associated with apoptosis but was responsible for mediating the inflammatory response. After the discovery of ICE, similar proteins to ICE were identified in
Peroxisomes, similar to the mitochondria, are a membranous subcellular organelle within eukaryotic cells. The peroxisome contains enzymes related to fatty acid and amino acid oxidation processes that produce hydrogen peroxide and also degrade hydrogen peroxide [25]. This gives the peroxisome its name and it plays an important role in maintaining intracellular oxidative metabolic homeostasis.
Because of the crucial role of the peroxisome, its dysfunction is associated with various pathological conditions, organ dysfunction, and aging [26, 27, 28]. For example, deficiency of Pex3, a peroxisomal membrane protein essential for membrane assembly, a member of the peroxisome (Pex) family, leads to complete loss of peroxisome function, while deficiency of Pex5, a peroxisome transporter, leads to Pex5 (a peroxisomal transporter) leads to the loss of peroxisomal matrix proteins. Mutations in this class of Pex genes may lead to human developmental abnormalities, such as human autosomal recessive disorders [29].
Peroxisomes play important roles in biosynthesis and signal transduction, which cannot be achieved without interaction with other organelles in the cell. In particular, peroxisomes interact functionally with mitochondria [30]. They cooperate with each other to perform biological functions such as production, fission, proliferation and degradation through vesicular transport, signaling, and membrane contact [31]. On the other hand, they can act synergistically to clear excess intracellular ROS, resist extracellular stresses through immune responses, and play an important role in the maintenance of lipid homeostasis through fatty acid β-oxidation [32, 33, 34]. In one word, peroxisomes are essential for the maintenance of normal mitochondrial and even whole cell function. Some chemotherapeutic drugs have been found to trigger mitochondrial dysfunction, leading to apoptosis by overwhelming cells with ROS. For example, Vorinostat (Vor), an FDA-approved histone deacetylase inhibitor (HDACi) for lymphoma treatment, has been well documented to trigger mitochondrial-mediated apoptosis through ROS accumulation. Acute Vor treatment has been shown to induce the expression of peroxisome proteins, thereby increasing peroxisome proliferation in a lymphoma model system. In addition, the knockdown of peroxisomes by gene silencing of Pex3 enhances Vor-induced ROS-mediated apoptosis [35].
In short, peroxisome dysfunction severely affects mitochondrial metabolism, cellular morphological stability, and biosynthesis, directly or indirectly contributing to a number of apoptosis-related diseases such as cancer [36, 37], cardiovascular disease [38, 39, 40], and neurodegenerative disorders [41].
Apoptosis is an important way for the organism to maintain the numerical homeostasis of the cell population. Excessive or insufficient apoptosis can lead to disease.
Crosstalk between mitochondria and other organelles is important in tumorigenesis. Mitochondria and peroxisomes are important organelles for ROS production and scavenging. Under normal conditions, both maintain intracellular ROS homeostasis. Impaired peroxisome function inevitably leads to increased levels of ROS in mitochondria, which impairs mitochondria, exacerbates impaired ROS clearance, leads to low levels of apoptosis, and thus promotes tumorigenesis and progression [42, 43, 44].
ROS act as signaling molecules to regulate various physiological and pathological processes [45]. H2O2 is a member of the ROS family and plays an important role in the signaling of epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). H2O2 prevents protein tyrosine phosphatase 1B (PTP1B) from dephosphorylating EGF, thereby facilitating EGF stimulation. In addition, activation of PDGF requires H2O2 to promote oxidation and inactivation of PDGF-receptor-associated phosphatases and SHP-2, thereby facilitating the signaling pathway [46, 47]. Excessive ROS production can lead to cellular genomic instability (including mutations in the mitochondrial genome) on the one hand. Notably, ROS can promote tumor cell proliferation under hypoxic conditions. The reason for this is that the transcription factors hypoxia-inducible factors (HIFs) are upregulated under hypoxic conditions, thus promoting the expression of oncogenes. Although some proteases such as prolyl hydroxylases (PHDs) can degrade HIFs, the increased release of ROS induced by hypoxia can prevent the action of PHDs on HIFs. In this case, HIFs can then promote tumor progression under hypoxic conditions.
Briefly, because disruption of the functional balance between mitochondria and peroxidases may lead to increased ROS production, the increased ROS may inhibit apoptosis-inducing genes (bcl2 and p53, etc.), resulting in non-apoptosis of cells that should be apoptotic. Alternatively, the apoptotic process may be inhibited due to a decrease in the activity of apoptosis-related enzymes (caspases, etc.), leading to malignant cell transformation and tissue malignant proliferation. Both of these aspects are considered to be one of the important mechanisms leading to tumorigenesis and infiltrative metastasis.
Apoptosis is a form of death of terminally differentiated cardiomyocytes. Clinical data suggest that ROS generation, DNA damage, and other factors activate apoptosis, resulting in the loss of large numbers of cardiomyocytes in patients with advanced congestive heart failure, patients with myocardial infarction, and patients with diabetic cardiomyopathy. The evidence suggests that apoptosis may be an important pathogenetic mechanism in cardiovascular disease [38]. Apoptosis, in concert with necrosis, may also lead to foam cell death and thus to the formation of a necrotic core, which contributes to lesion instability and increases the risk of lesion rupture and thrombosis.
Lower levels of ROS production can lead to chronic remodeling of the heart, whereas high levels of ROS can directly lead to apoptosis in the cardiomyocytes [48]. It is therefore interesting that catalase overexpression inhibits cardiomyocyte apoptosis by protecting the cells from ROS [49]. Peroxisomal antioxidant enzymes and plasmalogens protect cardiomyocytes via the degradation and trapping of ROS and the maintenance of ROS homeostasis. Apoptosis of cardiac cells has been demonstrated in several cardiovascular diseases, including myocardial ischemia–reperfusion injury (I/R) and atherosclerosis [50, 51, 52]. Atherosclerosis, a major cause of heart failure and myocardial infarction, can likewise predispose to acute coronary heart disease. There is evidence that thrombosis and plaque rupture may be due to apoptosis of a large number of smooth muscle cells and macrophages in unstable atherosclerotic plaques [53, 54]. Rupture of atherosclerotic plaques with concomitant thrombus formation may lead to coronary artery occlusion, which affects the blood supply to the myocardium, resulting in myocardial infarction and leading to patient death. Reperfusion is an effective treatment for acute myocardial infarction, but it may cause reperfusion injury while restoring blood flow [55]. Studies in the last decade or so have shown that cardiac cell death occurring during reperfusion after myocardial infarction is mainly apoptosis, not cell necrosis, which breaks the long-held misconception [56, 57, 58]. Usually, what occurs during I/R is mostly cell apoptosis, whereas necrosis occurs more often after prolonged ischemia. In addition, apoptosis also plays an important role in myocardial remodeling after infarction. There is evidence that a large number of apoptotic cells can be detected in myocardium at the marginal zone of myocardial infarction [56]. Since the regenerative capacity of myocardium is limited, people show great interest in preventing apoptosis of myocardial cells during I/R.
There is also a connection between chronic heart failure and apoptosis [59]. It has been reported that patients with advanced heart failure have higher rates of cardiac myocyte apoptosis than normal subjects. Using transgenic mice with cardiac tissue-specific expression of caspase-8, it was found that apoptosis of cardiomyocytes, even at very low levels, can lead to fatal dilated cardiomyopathy as long as it occurs chronically [60]. In addition, the use of caspase inhibitors prevented left ventricular dilatation and improved ventricular function, suggesting that long-term apoptosis can lead to a significant reduction in cardiomyocyte numbers, which in turn gradually decreases cardiac contractile function. As a result, the remaining cardiomyocytes become overcompensated and contribute to cardiac hypertrophy, leading to the development of heart failure [61].
Regarding the major pathways involved in apoptotic signaling in the heart, the death receptor pathway, the mitochondrial, and ER-stress death pathways are all involved [62]. The cross-talk between death receptors and mitochondrial cell death pathways has been demonstrated in cardiomyocytes and the heart [63, 64]. For example, Date
In recent years, ER stress pathway has been reported to be in cross-talk with both the death receptor pathway and the mitochondrial pathway [13, 67, 68]. One study found that application of TNF-α induced HL-1 myoblast cell lines that activated both caspase-3 and -12 [69]. Bcl-2, which targets ER, inhibited mitochondrial membrane depolarization in apoptotic cells and also inhibited cytochrome c release [70]. Caspase-8 cleaves BAP31, an ER-associated protein, and the cleaved fragment induces Ca2+ release from ER, into the mitochondria, and initiates apoptosis [71]. It has also been reported that Bik proteins can activate Bax/Bak in the ER membrane after localization to the mitochondria, initiating Ca2+ release [72].
Regardless of the causative factor, and regardless of which signal transduction pathway or pathways are involved, oxidative stress due to the interaction of peroxisomes and mitochondria plays a pivotal role in triggering apoptosis and thus contributing to the development of cardiovascular disease.
Apoptosis plays a key role in the normal development of the central nervous system and is involved in the pathogenesis of adult brain-related diseases, such as stroke [73] and neurodegenerative diseases [74].
There is growing evidence that the decline in peroxisome function with age may be associated with age-related neurodegenerative diseases such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) [75]. In the brains of patients with Alzheimer’s disease and Parkinson’s disease, plasmin levels are significantly reduced [76, 77], which suggests peroxisome dysfunction in neurodegenerative diseases. The lack of peroxisome activity in aged cells accumulates cellular ROS, which can compromise the integrity of organelles including mitochondria and the peroxisome itself. Subsequent defects in energy production mediated by peroxisomal fatty acid metabolism and mitochondrial oxidative phosphorylation may lead to metabolic failure in aged postmitotic cells, thereby inducing apoptosis associated with neurodegeneration.
Huntington’s disease (HD), a prototypical neurodegenerative disorder, is caused by a mutation in the Huntingtin protein due to a repeat amplification of the CAG in the Huntington gene. Patients with this disease suffer from neuronal dysfunction due to massive apoptosis of nerve cells, which in turn manifests as mental cognitive and motor impairment, and even disability [74].
ROS can easily poison neurons due to their series of characteristics, such as rich in fatty acids, easy intracellular production of large amounts of hydroxyl radicals, weak antioxidant capacity, and low regenerative capacity. In addition, because of the high metabolic rates, neurons require a high energy supply from mitochondria, which are both the most important intracellular organelle for ROS production and also vulnerable to ROS attack. It has been shown that treatment of isolated cultured cerebellar granule neurons with hydrogen peroxide induces mitochondrial fission within 1 hour [78]. Furthermore, treatment of mice with nitric oxide in stroke leads to massive fission of neuronal mitochondria before the onset of neuronal loss [79]. In the presence of calcium, acute exposure to high levels of ROS can induce massive opening of mitochondrial membrane transition pores and increased permeability, which in turn causes cell Apoptosis or necrosis occurs. ROS production in mitochondria forms a vicious cycle with oxidative stress and is toxic to cells. There is some evidence in transgenic mouse models of HD that showed that Tauroursodeoxycholic acid (TUDCA), a hydrophilic bile acid with antioxidant properties, prevents the production of reactive oxygen species, mitigates mitochondrial insufficiency and apoptosis, in part, by inhibiting Bax translocation from cytosol to the mitochondria [80]. TUDCA prevented striatal degeneration and ameliorated locomotor and cognitive deficits in a 3-NP (3-nitropropionic acid) rat model of HD. Keene
Apoptosis is a highly regulated cell death program that can be induced by a variety of physiological and pathological factors and has specific morphological and biochemical characteristics. The mechanism of its onset has not been completely elucidated to date, and it is now accepted that it is mediated by a number of pathways including the death receptor signaling pathway, the mitochondrial signaling pathway, and the endoplasmic reticulum signaling pathway. As an important way for the organism to maintain the numerical homeostasis of the cell population, apoptosis plays a key role in the pathogenesis of various human diseases. Peroxisomes and mitochondria are membrane-bound organelles in the cytoplasm of eukaryotic cells and are closely related to each other in their organelle synthesis and function. One of their important roles in cooperating with each other is to regulate the level and extent of apoptosis by maintaining the homeostasis of reactive oxygen species in the cell. Peroxisome dysfunction severely affects mitochondrial metabolism, cellular morphological stability, and biosynthesis, and therefore contributes directly or indirectly to a number of apoptosis-related diseases. Based on the available relevant findings, this chapter presents and summarizes the important potential role of peroxisomes in apoptosis-related diseases such as tumors, cardiovascular diseases, and neuropsychiatric disorders.
This work was supported in part by grants from National Natural Science Foundation of China (22176002), Anhui Provincial Natural Science Foundation (2008085 MB49), Natural Science Foundation of Anhui Provincial Department of Education (KJ2021A0215), Anhui Medical University Research Enhancement Program (2021xkjT004), and Open Project Fund of the Key Laboratory of the Ministry of Education for the Birth Population (JKZD20202).
The authors report no conflicts of interest.
IntechOpen publishes different types of publications
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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. in Chemistry in July 2000, and his Ph.D. in Physical Chemistry in 2007 from the University of Khartoum, Sudan. In 2009 he joined the Dr. Ron Clarke research group at the School of Chemistry, Faculty of Science, University of Sydney, Australia 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. He then worked as Assistant Professor at the Department of Chemistry, University of Khartoum, and in 2014 was promoted to Associate Professor ranking. In 2011 he joined the staff of the Chemistry Department at Taif University, Saudi Arabia, where he is currently active as an Assistant Professor. His research interests include:\r\n(1) P-type ATPase Enzyme Kinetics and Mechanisms; (2) Kinetics and Mechanism of Redox Reactions; (3) Autocatalytic reactions; (4) Computational enzyme kinetics; (5) Allosteric acceleration of P-type ATPases by ATP; (6) Exploring of allosteric sites of ATPases and interaction of ATP with ATPases located in the 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"}}}]}},subseries:{item:{id:"94",type:"subseries",title:"Climate Change and Environmental Sustainability",keywords:"Environmental protection, Socio-economic development, Resource exploitation, Environmental degradation, Climate change, Degraded ecosystems, Biodiversity loss",scope:"\r\n\tSustainable development focuses on linking economic development with environmental protection and social development to ensure future prosperity for people and the planet. To tackle global challenges of development and environment, the United Nations General Assembly in 2015 adopted the 17 Sustainable Development Goals. SDGs emphasize that environmental sustainability should be strongly linked to socio-economic development, which should be decoupled from escalating resource use and environmental degradation for the purpose of reducing environmental stress, enhancing human welfare, and improving regional equity. Moreover, sustainable development seeks a balance between human development and decrease in ecological/environmental marginal benefits. Under the increasing stress of climate change, many environmental problems have emerged causing severe impacts at both global and local scales, driving ecosystem service reduction and biodiversity loss. Humanity’s relationship with resource exploitation and environment protection is a major global concern, as new threats to human and environmental security emerge in the Anthropocene. Currently, the world is facing significant challenges in environmental sustainability to protect global environments and to restore degraded ecosystems, while maintaining human development with regional equality. Thus, environmental sustainability with healthy natural ecosystems is critical to maintaining human prosperity in our warming planet.
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