Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics.
Identifieur interne : 000C97 ( PubMed/Curation ); précédent : 000C96; suivant : 000C98Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics.
Auteurs : I. Irrcher [Canada] ; H. Aleyasin ; E L Seifert ; S J Hewitt ; S. Chhabra ; M. Phillips ; A K Lutz ; M W C. Rousseaux ; L. Bevilacqua ; A. Jahani-Asl ; S. Callaghan ; J G Maclaurin ; K F Winklhofer ; P. Rizzu ; P. Rippstein ; R H Kim ; C X Chen ; E A Fon ; R S Slack ; M E Harper ; H M Mcbride ; T W Mak ; D S ParkSource :
- Human molecular genetics [ 1460-2083 ] ; 2010.
English descriptors
- KwdEn :
- Acetylcysteine (pharmacology), Animals, Autophagy (drug effects), Brain (metabolism), Brain (pathology), Cell Death (drug effects), Cell Line, Humans, Intracellular Signaling Peptides and Proteins (deficiency), Intracellular Signaling Peptides and Proteins (genetics), Mice, Mitochondria (drug effects), Mitochondria (genetics), Mitochondria (pathology), Mitochondria (ultrastructure), Mutant Proteins (metabolism), Neostriatum (drug effects), Neostriatum (metabolism), Neostriatum (pathology), Neostriatum (ultrastructure), Neurons (drug effects), Neurons (enzymology), Neurons (pathology), Neurons (ultrastructure), Oncogene Proteins (deficiency), Oncogene Proteins (genetics), Parkinson Disease (genetics), Parkinson Disease (pathology), Peroxiredoxins, Phenotype, Protein Deglycase DJ-1, Protein Kinases (metabolism), Reactive Oxygen Species (metabolism), Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , deficiency : Intracellular Signaling Peptides and Proteins, Oncogene Proteins.
- chemical , genetics : Intracellular Signaling Peptides and Proteins, Oncogene Proteins.
- chemical , metabolism : Mutant Proteins, Protein Kinases, Reactive Oxygen Species, Ubiquitin-Protein Ligases.
- chemical , pharmacology : Acetylcysteine.
- drug effects : Autophagy, Cell Death, Mitochondria, Neostriatum, Neurons.
- enzymology : Neurons.
- genetics : Mitochondria, Parkinson Disease.
- metabolism : Brain, Neostriatum.
- pathology : Brain, Mitochondria, Neostriatum, Neurons, Parkinson Disease.
- ultrastructure : Mitochondria, Neostriatum, Neurons.
- Animals, Cell Line, Humans, Mice, Peroxiredoxins, Phenotype, Protein Deglycase DJ-1.
Abstract
Growing evidence highlights a role for mitochondrial dysfunction and oxidative stress as underlying contributors to Parkinson's disease (PD) pathogenesis. DJ-1 (PARK7) is a recently identified recessive familial PD gene. Its loss leads to increased susceptibility of neurons to oxidative stress and death. However, its mechanism of action is not fully understood. Presently, we report that DJ-1 deficiency in cell lines, cultured neurons, mouse brain and lymphoblast cells derived from DJ-1 patients display aberrant mitochondrial morphology. We also show that these DJ-1-dependent mitochondrial defects contribute to oxidative stress-induced sensitivity to cell death since reversal of this fragmented mitochondrial phenotype abrogates neuronal cell death. Reactive oxygen species (ROS) appear to play a critical role in the observed defects, as ROS scavengers rescue the phenotype and mitochondria isolated from DJ-1 deficient animals produce more ROS compared with control. Importantly, the aberrant mitochondrial phenotype can be rescued by the expression of Pink1 and Parkin, two PD-linked genes involved in regulating mitochondrial dynamics and quality control. Finally, we show that DJ-1 deficiency leads to altered autophagy in murine and human cells. Our findings define a mechanism by which the DJ-1-dependent mitochondrial defects contribute to the increased sensitivity to oxidative stress-induced cell death that has been previously reported.
DOI: 10.1093/hmg/ddq288
PubMed: 20639397
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Irrcher</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa</wicri:regionArea></affiliation></author><author><name sortKey="Aleyasin, H" sort="Aleyasin, H" uniqKey="Aleyasin H" first="H" last="Aleyasin">H. Aleyasin</name></author><author><name sortKey="Seifert, E L" sort="Seifert, E L" uniqKey="Seifert E" first="E L" last="Seifert">E L Seifert</name></author><author><name sortKey="Hewitt, S J" sort="Hewitt, S J" uniqKey="Hewitt S" first="S J" last="Hewitt">S J Hewitt</name></author><author><name sortKey="Chhabra, S" sort="Chhabra, S" uniqKey="Chhabra S" first="S" last="Chhabra">S. Chhabra</name></author><author><name sortKey="Phillips, M" sort="Phillips, M" uniqKey="Phillips M" first="M" last="Phillips">M. 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DJ-1 (PARK7) is a recently identified recessive familial PD gene. Its loss leads to increased susceptibility of neurons to oxidative stress and death. However, its mechanism of action is not fully understood. Presently, we report that DJ-1 deficiency in cell lines, cultured neurons, mouse brain and lymphoblast cells derived from DJ-1 patients display aberrant mitochondrial morphology. We also show that these DJ-1-dependent mitochondrial defects contribute to oxidative stress-induced sensitivity to cell death since reversal of this fragmented mitochondrial phenotype abrogates neuronal cell death. Reactive oxygen species (ROS) appear to play a critical role in the observed defects, as ROS scavengers rescue the phenotype and mitochondria isolated from DJ-1 deficient animals produce more ROS compared with control. Importantly, the aberrant mitochondrial phenotype can be rescued by the expression of Pink1 and Parkin, two PD-linked genes involved in regulating mitochondrial dynamics and quality control. Finally, we show that DJ-1 deficiency leads to altered autophagy in murine and human cells. Our findings define a mechanism by which the DJ-1-dependent mitochondrial defects contribute to the increased sensitivity to oxidative stress-induced cell death that has been previously reported.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20639397</PMID><DateCreated><Year>2010</Year><Month>09</Month><Day>09</Day></DateCreated><DateCompleted><Year>2011</Year><Month>01</Month><Day>04</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2083</ISSN><JournalIssue CitedMedium="Internet"><Volume>19</Volume><Issue>19</Issue><PubDate><Year>2010</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>Human molecular genetics</Title><ISOAbbreviation>Hum. Mol. Genet.</ISOAbbreviation></Journal><ArticleTitle>Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics.</ArticleTitle><Pagination><MedlinePgn>3734-46</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/hmg/ddq288</ELocationID><Abstract><AbstractText>Growing evidence highlights a role for mitochondrial dysfunction and oxidative stress as underlying contributors to Parkinson's disease (PD) pathogenesis. DJ-1 (PARK7) is a recently identified recessive familial PD gene. Its loss leads to increased susceptibility of neurons to oxidative stress and death. However, its mechanism of action is not fully understood. Presently, we report that DJ-1 deficiency in cell lines, cultured neurons, mouse brain and lymphoblast cells derived from DJ-1 patients display aberrant mitochondrial morphology. We also show that these DJ-1-dependent mitochondrial defects contribute to oxidative stress-induced sensitivity to cell death since reversal of this fragmented mitochondrial phenotype abrogates neuronal cell death. Reactive oxygen species (ROS) appear to play a critical role in the observed defects, as ROS scavengers rescue the phenotype and mitochondria isolated from DJ-1 deficient animals produce more ROS compared with control. Importantly, the aberrant mitochondrial phenotype can be rescued by the expression of Pink1 and Parkin, two PD-linked genes involved in regulating mitochondrial dynamics and quality control. Finally, we show that DJ-1 deficiency leads to altered autophagy in murine and human cells. Our findings define a mechanism by which the DJ-1-dependent mitochondrial defects contribute to the increased sensitivity to oxidative stress-induced cell death that has been previously reported.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Irrcher</LastName><ForeName>I</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aleyasin</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Seifert</LastName><ForeName>E L</ForeName><Initials>EL</Initials></Author><Author ValidYN="Y"><LastName>Hewitt</LastName><ForeName>S J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Chhabra</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Phillips</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Lutz</LastName><ForeName>A K</ForeName><Initials>AK</Initials></Author><Author ValidYN="Y"><LastName>Rousseaux</LastName><ForeName>M W C</ForeName><Initials>MW</Initials></Author><Author ValidYN="Y"><LastName>Bevilacqua</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Jahani-Asl</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Callaghan</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>MacLaurin</LastName><ForeName>J G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Winklhofer</LastName><ForeName>K F</ForeName><Initials>KF</Initials></Author><Author ValidYN="Y"><LastName>Rizzu</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Rippstein</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>R H</ForeName><Initials>RH</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>C X</ForeName><Initials>CX</Initials></Author><Author ValidYN="Y"><LastName>Fon</LastName><ForeName>E A</ForeName><Initials>EA</Initials></Author><Author ValidYN="Y"><LastName>Slack</LastName><ForeName>R S</ForeName><Initials>RS</Initials></Author><Author ValidYN="Y"><LastName>Harper</LastName><ForeName>M E</ForeName><Initials>ME</Initials></Author><Author ValidYN="Y"><LastName>McBride</LastName><ForeName>H M</ForeName><Initials>HM</Initials></Author><Author ValidYN="Y"><LastName>Mak</LastName><ForeName>T W</ForeName><Initials>TW</Initials></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>D S</ForeName><Initials>DS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Canadian Institutes of Health Research</Agency><Country>Canada</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>07</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Hum Mol Genet</MedlineTA><NlmUniqueID>9208958</NlmUniqueID><ISSNLinking>0964-6906</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047908">Intracellular Signaling Peptides and Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015513">Oncogene 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MajorTopicYN="N">Protein Deglycase DJ-1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20639397</ArticleId><ArticleId IdType="pii">ddq288</ArticleId><ArticleId IdType="doi">10.1093/hmg/ddq288</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics.
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