Autophagy and apoptosis dysfunction in neurodegenerative disorders.
Identifieur interne : 000828 ( PubMed/Curation ); précédent : 000827; suivant : 000829Autophagy and apoptosis dysfunction in neurodegenerative disorders.
Auteurs : Saeid Ghavami [Canada] ; Shahla Shojaei [Iran] ; Behzad Yeganeh [Canada] ; Sudharsana R. Ande [Canada] ; Jaganmohan R. Jangamreddy [Suède] ; Maryam Mehrpour [France] ; Jonas Christoffersson [Suède] ; Wiem Chaabane [Tunisie] ; Adel Rezaei Moghadam [Iran] ; Hessam H. Kashani [Canada] ; Mohammad Hashemi [Iran] ; Ali A. Owji [Iran] ; Marek J. Łos [Suède]Source :
- Progress in neurobiology [ 1873-5118 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Apoptosis, Autophagy, Brain (pathology), Brain (physiopathology), Brain Diseases (pathology), Brain Diseases (physiopathology), Humans, Neurodegenerative Diseases (pathology), Neurodegenerative Diseases (physiopathology), Neurons (pathology), Peripheral Nervous System Diseases (pathology), Peripheral Nervous System Diseases (physiopathology).
- MESH :
- pathology : Brain, Brain Diseases, Neurodegenerative Diseases, Neurons, Peripheral Nervous System Diseases.
- physiopathology : Brain, Brain Diseases, Neurodegenerative Diseases, Peripheral Nervous System Diseases.
- Animals, Apoptosis, Autophagy, Humans.
Abstract
Autophagy and apoptosis are basic physiologic processes contributing to the maintenance of cellular homeostasis. Autophagy encompasses pathways that target long-lived cytosolic proteins and damaged organelles. It involves a sequential set of events including double membrane formation, elongation, vesicle maturation and finally delivery of the targeted materials to the lysosome. Apoptotic cell death is best described through its morphology. It is characterized by cell rounding, membrane blebbing, cytoskeletal collapse, cytoplasmic condensation, and fragmentation, nuclear pyknosis, chromatin condensation/fragmentation, and formation of membrane-enveloped apoptotic bodies, that are rapidly phagocytosed by macrophages or neighboring cells. Neurodegenerative disorders are becoming increasingly prevalent, especially in the Western societies, with larger percentage of members living to an older age. They have to be seen not only as a health problem, but since they are care-intensive, they also carry a significant economic burden. Deregulation of autophagy plays a pivotal role in the etiology and/or progress of many of these diseases. Herein, we briefly review the latest findings that indicate the involvement of autophagy in neurodegenerative diseases. We provide a brief introduction to autophagy and apoptosis pathways focusing on the role of mitochondria and lysosomes. We then briefly highlight pathophysiology of common neurodegenerative disorders like Alzheimer's diseases, Parkinson's disease, Huntington's disease and Amyotrophic lateral sclerosis. Then, we describe functions of autophagy and apoptosis in brain homeostasis, especially in the context of the aforementioned disorders. Finally, we discuss different ways that autophagy and apoptosis modulation may be employed for therapeutic intervention during the maintenance of neurodegenerative disorders.
DOI: 10.1016/j.pneurobio.2013.10.004
PubMed: 24211851
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Ande</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine, University of Manitoba, Winnipeg, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Internal Medicine, University of Manitoba, Winnipeg</wicri:regionArea></affiliation></author><author><name sortKey="Jangamreddy, Jaganmohan R" sort="Jangamreddy, Jaganmohan R" uniqKey="Jangamreddy J" first="Jaganmohan R" last="Jangamreddy">Jaganmohan R. Jangamreddy</name><affiliation wicri:level="1"><nlm:affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping</wicri:regionArea></affiliation></author><author><name sortKey="Mehrpour, Maryam" sort="Mehrpour, Maryam" uniqKey="Mehrpour M" first="Maryam" last="Mehrpour">Maryam Mehrpour</name><affiliation wicri:level="1"><nlm:affiliation>INSERM U845, Research Center "Growth & Signaling" Paris Descartes University Medical School, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>INSERM U845, Research Center "Growth & Signaling" Paris Descartes University Medical School</wicri:regionArea></affiliation></author><author><name sortKey="Christoffersson, Jonas" sort="Christoffersson, Jonas" uniqKey="Christoffersson J" first="Jonas" last="Christoffersson">Jonas Christoffersson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping</wicri:regionArea></affiliation></author><author><name sortKey="Chaabane, Wiem" sort="Chaabane, Wiem" uniqKey="Chaabane W" first="Wiem" last="Chaabane">Wiem Chaabane</name><affiliation wicri:level="1"><nlm:affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden; Department of Biology, Faculty of Sciences, Tunis University, Tunis, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden; Department of Biology, Faculty of Sciences, Tunis University, Tunis</wicri:regionArea></affiliation></author><author><name sortKey="Moghadam, Adel Rezaei" sort="Moghadam, Adel Rezaei" uniqKey="Moghadam A" first="Adel Rezaei" last="Moghadam">Adel Rezaei Moghadam</name><affiliation wicri:level="1"><nlm:affiliation>Young Researchers Club, Ardabil Branch, Islamic Azad University, Ardabil, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Young Researchers Club, Ardabil Branch, Islamic Azad University, Ardabil</wicri:regionArea></affiliation></author><author><name sortKey="Kashani, Hessam H" sort="Kashani, Hessam H" uniqKey="Kashani H" first="Hessam H" last="Kashani">Hessam H. Kashani</name><affiliation wicri:level="1"><nlm:affiliation>Department of Human Anatomy and Cell Science, University of Manitoba, Winnipeg, Canada; Manitoba Institute of Child Health, Department of Physiology, University of Manitoba, Winnipeg, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Human Anatomy and Cell Science, University of Manitoba, Winnipeg, Canada; Manitoba Institute of Child Health, Department of Physiology, University of Manitoba, Winnipeg</wicri:regionArea></affiliation></author><author><name sortKey="Hashemi, Mohammad" sort="Hashemi, Mohammad" uniqKey="Hashemi M" first="Mohammad" last="Hashemi">Mohammad Hashemi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran; Cellular and Molecular Biology Research Center, Zahedan University of Medical Sciences, Zahedan, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran; Cellular and Molecular Biology Research Center, Zahedan University of Medical Sciences, Zahedan</wicri:regionArea></affiliation></author><author><name sortKey="Owji, Ali A" sort="Owji, Ali A" uniqKey="Owji A" first="Ali A" last="Owji">Ali A. Owji</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Recombinant Protein Laboratory, Medical School, Shiraz University of Medical Sciences, Shiraz, Iran. Electronic address: aaowji@yahoo.com.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Department of Biochemistry, Recombinant Protein Laboratory, Medical School, Shiraz University of Medical Sciences, Shiraz</wicri:regionArea></affiliation></author><author><name sortKey="Los, Marek J" sort="Los, Marek J" uniqKey="Los M" first="Marek J" last="Łos">Marek J. Łos</name><affiliation wicri:level="1"><nlm:affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden. Electronic address: mjelos@gmail.com.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping</wicri:regionArea></affiliation></author></analytic><series><title level="j">Progress in neurobiology</title><idno type="eISSN">1873-5118</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Autophagy</term><term>Brain (pathology)</term><term>Brain (physiopathology)</term><term>Brain Diseases (pathology)</term><term>Brain Diseases (physiopathology)</term><term>Humans</term><term>Neurodegenerative Diseases (pathology)</term><term>Neurodegenerative Diseases (physiopathology)</term><term>Neurons (pathology)</term><term>Peripheral Nervous System Diseases (pathology)</term><term>Peripheral Nervous System Diseases (physiopathology)</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term><term>Brain Diseases</term><term>Neurodegenerative Diseases</term><term>Neurons</term><term>Peripheral Nervous System Diseases</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Brain</term><term>Brain Diseases</term><term>Neurodegenerative Diseases</term><term>Peripheral Nervous System Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Autophagy</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagy and apoptosis are basic physiologic processes contributing to the maintenance of cellular homeostasis. Autophagy encompasses pathways that target long-lived cytosolic proteins and damaged organelles. It involves a sequential set of events including double membrane formation, elongation, vesicle maturation and finally delivery of the targeted materials to the lysosome. Apoptotic cell death is best described through its morphology. It is characterized by cell rounding, membrane blebbing, cytoskeletal collapse, cytoplasmic condensation, and fragmentation, nuclear pyknosis, chromatin condensation/fragmentation, and formation of membrane-enveloped apoptotic bodies, that are rapidly phagocytosed by macrophages or neighboring cells. Neurodegenerative disorders are becoming increasingly prevalent, especially in the Western societies, with larger percentage of members living to an older age. They have to be seen not only as a health problem, but since they are care-intensive, they also carry a significant economic burden. Deregulation of autophagy plays a pivotal role in the etiology and/or progress of many of these diseases. Herein, we briefly review the latest findings that indicate the involvement of autophagy in neurodegenerative diseases. We provide a brief introduction to autophagy and apoptosis pathways focusing on the role of mitochondria and lysosomes. We then briefly highlight pathophysiology of common neurodegenerative disorders like Alzheimer's diseases, Parkinson's disease, Huntington's disease and Amyotrophic lateral sclerosis. Then, we describe functions of autophagy and apoptosis in brain homeostasis, especially in the context of the aforementioned disorders. Finally, we discuss different ways that autophagy and apoptosis modulation may be employed for therapeutic intervention during the maintenance of neurodegenerative disorders.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24211851</PMID><DateCreated><Year>2013</Year><Month>12</Month><Day>23</Day></DateCreated><DateCompleted><Year>2014</Year><Month>08</Month><Day>16</Day></DateCompleted><DateRevised><Year>2013</Year><Month>12</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>112</Volume><PubDate><Year>2014</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Progress in neurobiology</Title><ISOAbbreviation>Prog. Neurobiol.</ISOAbbreviation></Journal><ArticleTitle>Autophagy and apoptosis dysfunction in neurodegenerative disorders.</ArticleTitle><Pagination><MedlinePgn>24-49</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.pneurobio.2013.10.004</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0301-0082(13)00104-4</ELocationID><Abstract><AbstractText>Autophagy and apoptosis are basic physiologic processes contributing to the maintenance of cellular homeostasis. Autophagy encompasses pathways that target long-lived cytosolic proteins and damaged organelles. It involves a sequential set of events including double membrane formation, elongation, vesicle maturation and finally delivery of the targeted materials to the lysosome. Apoptotic cell death is best described through its morphology. It is characterized by cell rounding, membrane blebbing, cytoskeletal collapse, cytoplasmic condensation, and fragmentation, nuclear pyknosis, chromatin condensation/fragmentation, and formation of membrane-enveloped apoptotic bodies, that are rapidly phagocytosed by macrophages or neighboring cells. Neurodegenerative disorders are becoming increasingly prevalent, especially in the Western societies, with larger percentage of members living to an older age. They have to be seen not only as a health problem, but since they are care-intensive, they also carry a significant economic burden. Deregulation of autophagy plays a pivotal role in the etiology and/or progress of many of these diseases. Herein, we briefly review the latest findings that indicate the involvement of autophagy in neurodegenerative diseases. We provide a brief introduction to autophagy and apoptosis pathways focusing on the role of mitochondria and lysosomes. We then briefly highlight pathophysiology of common neurodegenerative disorders like Alzheimer's diseases, Parkinson's disease, Huntington's disease and Amyotrophic lateral sclerosis. Then, we describe functions of autophagy and apoptosis in brain homeostasis, especially in the context of the aforementioned disorders. Finally, we discuss different ways that autophagy and apoptosis modulation may be employed for therapeutic intervention during the maintenance of neurodegenerative disorders.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ghavami</LastName><ForeName>Saeid</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Human Anatomy and Cell Science, University of Manitoba, Winnipeg, Canada; Manitoba Institute of Child Health, Department of Physiology, University of Manitoba, Winnipeg, Canada; St. Boniface Research Centre, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shojaei</LastName><ForeName>Shahla</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Recombinant Protein Laboratory, Medical School, Shiraz University of Medical Sciences, Shiraz, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yeganeh</LastName><ForeName>Behzad</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Manitoba Institute of Child Health, Department of Physiology, University of Manitoba, Winnipeg, Canada; Hospital for Sick Children Research Institute, Department of Physiology and Experimental Medicine, University of Toronto, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ande</LastName><ForeName>Sudharsana R</ForeName><Initials>SR</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jangamreddy</LastName><ForeName>Jaganmohan R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mehrpour</LastName><ForeName>Maryam</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>INSERM U845, Research Center "Growth & Signaling" Paris Descartes University Medical School, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Christoffersson</LastName><ForeName>Jonas</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaabane</LastName><ForeName>Wiem</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden; Department of Biology, Faculty of Sciences, Tunis University, Tunis, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moghadam</LastName><ForeName>Adel Rezaei</ForeName><Initials>AR</Initials><AffiliationInfo><Affiliation>Young Researchers Club, Ardabil Branch, Islamic Azad University, Ardabil, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kashani</LastName><ForeName>Hessam H</ForeName><Initials>HH</Initials><AffiliationInfo><Affiliation>Department of Human Anatomy and Cell Science, University of Manitoba, Winnipeg, Canada; Manitoba Institute of Child Health, Department of Physiology, University of Manitoba, Winnipeg, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hashemi</LastName><ForeName>Mohammad</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran; Cellular and Molecular Biology Research Center, Zahedan University of Medical Sciences, Zahedan, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Owji</LastName><ForeName>Ali A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Recombinant Protein Laboratory, Medical School, Shiraz University of Medical Sciences, Shiraz, Iran. Electronic address: aaowji@yahoo.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Łos</LastName><ForeName>Marek J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Department of Clinical and Experimental Medicine (IKE), Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linkoping University, Linkoping, Sweden. Electronic address: mjelos@gmail.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>11</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Prog Neurobiol</MedlineTA><NlmUniqueID>0370121</NlmUniqueID><ISSNLinking>0301-0082</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="Y">Apoptosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001927" MajorTopicYN="N">Brain Diseases</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010523" MajorTopicYN="N">Peripheral Nervous System Diseases</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">AD</Keyword><Keyword MajorTopicYN="N">AIF</Keyword><Keyword MajorTopicYN="N">ALS</Keyword><Keyword MajorTopicYN="N">AMBRA</Keyword><Keyword MajorTopicYN="N">AMP-activated protein kinase</Keyword><Keyword MajorTopicYN="N">AMPA</Keyword><Keyword MajorTopicYN="N">AMPK</Keyword><Keyword MajorTopicYN="N">APP</Keyword><Keyword MajorTopicYN="N">ATG</Keyword><Keyword MajorTopicYN="N">Alzheimer's diseases</Keyword><Keyword MajorTopicYN="N">Apo-E</Keyword><Keyword MajorTopicYN="N">Aβ</Keyword><Keyword MajorTopicYN="N">BDNF</Keyword><Keyword MajorTopicYN="N">CMA</Keyword><Keyword MajorTopicYN="N">ER</Keyword><Keyword MajorTopicYN="N">ESCRT</Keyword><Keyword MajorTopicYN="N">HD</Keyword><Keyword MajorTopicYN="N">HEK293</Keyword><Keyword MajorTopicYN="N">HIP-1</Keyword><Keyword MajorTopicYN="N">Htt</Keyword><Keyword MajorTopicYN="N">Huntingtin interacting protein</Keyword><Keyword MajorTopicYN="N">Huntingtin protein</Keyword><Keyword MajorTopicYN="N">Huntington's disease</Keyword><Keyword MajorTopicYN="N">InsP(6)Ks</Keyword><Keyword MajorTopicYN="N">LAMP</Keyword><Keyword MajorTopicYN="N">LC3</Keyword><Keyword MajorTopicYN="N">LRPPRC</Keyword><Keyword MajorTopicYN="N">MAP15</Keyword><Keyword MajorTopicYN="N">Mitochondria dysfunction</Keyword><Keyword MajorTopicYN="N">N-methyl-d-aspartate</Keyword><Keyword MajorTopicYN="N">NCCD</Keyword><Keyword MajorTopicYN="N">NMDA</Keyword><Keyword MajorTopicYN="N">PCD</Keyword><Keyword MajorTopicYN="N">PD</Keyword><Keyword MajorTopicYN="N">PINK-1</Keyword><Keyword MajorTopicYN="N">PON 1–3</Keyword><Keyword MajorTopicYN="N">PTEN-induced putative kinase 1</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Porteopathies</Keyword><Keyword MajorTopicYN="N">RCAN-1</Keyword><Keyword MajorTopicYN="N">RSVA314</Keyword><Keyword MajorTopicYN="N">RSVA405</Keyword><Keyword MajorTopicYN="N">RUBICON</Keyword><Keyword MajorTopicYN="N">RUN domain and cysteine rich domain containing</Keyword><Keyword MajorTopicYN="N">Resveratrol</Keyword><Keyword MajorTopicYN="N">TAR DNA-binding protein 43kDa</Keyword><Keyword MajorTopicYN="N">TDP-43-kDa</Keyword><Keyword MajorTopicYN="N">Trehalose</Keyword><Keyword MajorTopicYN="N">UPS</Keyword><Keyword MajorTopicYN="N">UVRAG</Keyword><Keyword MajorTopicYN="N">VCP</Keyword><Keyword MajorTopicYN="N">X-box binding protein-1</Keyword><Keyword MajorTopicYN="N">XBP-1</Keyword><Keyword MajorTopicYN="N">activating molecule in Beclin-1-regulated autophagy</Keyword><Keyword MajorTopicYN="N">alpha-synuclein</Keyword><Keyword MajorTopicYN="N">amyloid beta precursor protein</Keyword><Keyword MajorTopicYN="N">amyloid-beta</Keyword><Keyword MajorTopicYN="N">amyotrophic lateral sclerosis</Keyword><Keyword MajorTopicYN="N">apolipo-protein E</Keyword><Keyword MajorTopicYN="N">apoptosis-inducing factor</Keyword><Keyword MajorTopicYN="N">autophagosome-associated light chain 3</Keyword><Keyword MajorTopicYN="N">autphagy related genes</Keyword><Keyword MajorTopicYN="N">brain-derived neurotrophic factor</Keyword><Keyword MajorTopicYN="N">chaperon-mediated autophagy</Keyword><Keyword MajorTopicYN="N">endoplasmic reticulum</Keyword><Keyword MajorTopicYN="N">endosomal sorting complexes required for transport</Keyword><Keyword MajorTopicYN="N">human embryonic kidney 293 cells</Keyword><Keyword MajorTopicYN="N">inositol hexakisphosphate kinases</Keyword><Keyword MajorTopicYN="N">lysosomal associated membrane proteins</Keyword><Keyword MajorTopicYN="N">mHtt</Keyword><Keyword MajorTopicYN="N">mPTP</Keyword><Keyword MajorTopicYN="N">mTOR</Keyword><Keyword MajorTopicYN="N">mammalian target of rapamycin</Keyword><Keyword MajorTopicYN="N">microtubule-associated protein 15</Keyword><Keyword MajorTopicYN="N">mitochondrial permeability transition pore</Keyword><Keyword MajorTopicYN="N">mitochondrion-associated leucine-rich PPR-motif containing protein</Keyword><Keyword MajorTopicYN="N">mutant Huntingtin protein</Keyword><Keyword MajorTopicYN="N">nomenclature committee on cell death</Keyword><Keyword MajorTopicYN="N">p53</Keyword><Keyword MajorTopicYN="N">pQ</Keyword><Keyword MajorTopicYN="N">paraxonase enzymes</Keyword><Keyword MajorTopicYN="N">poly-glutamine</Keyword><Keyword MajorTopicYN="N">programmed cell death</Keyword><Keyword MajorTopicYN="N">regulator of calcineurin-1</Keyword><Keyword MajorTopicYN="N">tumor protein 53</Keyword><Keyword MajorTopicYN="N">ubiquitin-proteasome system</Keyword><Keyword MajorTopicYN="N">ultra-violet radiation resistance-associated gene</Keyword><Keyword MajorTopicYN="N">valosin-containing protein</Keyword><Keyword MajorTopicYN="N">α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid</Keyword><Keyword MajorTopicYN="N">α-syn</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>12</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>10</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>8</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24211851</ArticleId><ArticleId IdType="pii">S0301-0082(13)00104-4</ArticleId><ArticleId IdType="doi">10.1016/j.pneurobio.2013.10.004</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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