Rapamycin protects against rotenone-induced apoptosis through autophagy induction.
Identifieur interne : 000110 ( PubMed/Checkpoint ); précédent : 000109; suivant : 000111Rapamycin protects against rotenone-induced apoptosis through autophagy induction.
Auteurs : T. Pan [États-Unis] ; P. Rawal ; Y. Wu ; W. Xie ; Joseph Jankovic [États-Unis] ; W. LeSource :
- Neuroscience ; 2009.
English descriptors
- KwdEn :
- Apoptosis (drug effects), Apoptosis (physiology), Autophagy (drug effects), Autophagy (physiology), Cell Line, Tumor, Cytochromes c (metabolism), Cytoplasm (drug effects), Cytoplasm (physiology), Cytoplasm (ultrastructure), Electron Transport Complex IV (metabolism), Humans, Insecticides (toxicity), Microtubule-Associated Proteins (metabolism), Mitochondria (drug effects), Mitochondria (physiology), Mitochondria (ultrastructure), Neuroprotective Agents (pharmacology), RNA, Small Interfering (metabolism), Rotenone (toxicity), Sirolimus (pharmacology), Ubiquitinated Proteins (metabolism).
- MESH :
- chemical , metabolism : Cytochromes c, Electron Transport Complex IV, Microtubule-Associated Proteins, RNA, Small Interfering, Ubiquitinated Proteins.
- drug effects : Apoptosis, Autophagy, Cytoplasm, Mitochondria.
- chemical , pharmacology : Neuroprotective Agents, Sirolimus.
- physiology : Apoptosis, Autophagy, Cytoplasm, Mitochondria.
- chemical , toxicity : Insecticides, Rotenone.
- ultrastructure : Cytoplasm, Mitochondria.
- Cell Line, Tumor, Humans.
Abstract
Ubiquitin proteasome system (UPS) and autophagy lysosome pathway (ALP) are the two most important routes for degradation of aggregated/misfolded proteins. Additionally, ALP is so far the only known route to clear entire organelles, such as mitochondria. We proposed that enhancement of ALP may be beneficial for some neurodegenerative disorders, such as Parkinson's disease (PD), in which the accumulation of aggregated/misfolded proteins and the dysfunction of mitochondria are the two major pathogenesis. Mitochondrial complex I inhibitor rotenone, which causes dysfunction mitochondria and UPS, has been considered as one of the neurotoxins related to PD. In this study, rotenone-exposed human neuronal SH-SY5Y cells were used as an in vitro model for us to determine whether autophagy enhancer rapamycin could protect against rotenone-induced injury and its underlying mechanisms. The observed results showed that rapamycin alleviated rotenone-induced apoptosis, whose effects were partially blocked when autophagy related gene 5 (Atg5) was suppressed by Atg5 small interference RNA (siRNA) transfection. Additionally, the results showed that rapamycin pretreatment diminished rotenone-induced accumulation of high molecular weight ubiquitinated bands, and reduced rotenone-induced increase of cytochrome c in cytosolic fraction and decreased mitochondrial marker cytochrome oxidase subunit IV (COX IV) in mitochondrial fraction. The changes in cytochrome c and COX IV indicated that the decreased translocation of cytochrome c from mitochondria to cytosol was probably due to the turn over of entire injured mitochondria. The results that lysosome and mitochondria were colocolized within the cells pretreated with rapamycin and that the mitochondria could be found within autophagy double membrane structures further supported that the damaged mitochondria might be cleared through autophagy, which process has been termed as "mitophagy." Our studies suggested that autophagy enhancer rapamycin is neuroprotective against rotenone-induced apoptosis through autophagy enhancement. We concluded that pharmacologically induction of autophagy by rapamycin may represent a useful therapeutic strategy as disease-modifiers in PD.
DOI: 10.1016/j.neuroscience.2009.08.014
PubMed: 19682553
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Rapamycin protects against rotenone-induced apoptosis through autophagy induction.</title><author><name sortKey="Pan, T" sort="Pan, T" uniqKey="Pan T" first="T" last="Pan">T. Pan</name><affiliation wicri:level="2"><nlm:affiliation>Parkinson Disease Research Laboratory, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Parkinson Disease Research Laboratory, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Rawal, P" sort="Rawal, P" uniqKey="Rawal P" first="P" last="Rawal">P. Rawal</name></author><author><name sortKey="Wu, Y" sort="Wu, Y" uniqKey="Wu Y" first="Y" last="Wu">Y. Wu</name></author><author><name sortKey="Xie, W" sort="Xie, W" uniqKey="Xie W" first="W" last="Xie">W. Xie</name></author><author><name sortKey="Jankovic, J" sort="Jankovic, J" uniqKey="Jankovic J" first="J" last="Jankovic">Joseph Jankovic</name><affiliation><country>États-Unis</country><placeName><settlement type="city">Houston</settlement><region type="state">Texas</region></placeName><orgName type="university" n="3">Baylor College of Medicine</orgName></affiliation></author><author><name sortKey="Le, W" sort="Le, W" uniqKey="Le W" first="W" last="Le">W. Le</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="doi">10.1016/j.neuroscience.2009.08.014</idno><idno type="RBID">pubmed:19682553</idno><idno type="pmid">19682553</idno><idno type="wicri:Area/PubMed/Corpus">000114</idno><idno type="wicri:Area/PubMed/Curation">000114</idno><idno type="wicri:Area/PubMed/Checkpoint">000110</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Rapamycin protects against rotenone-induced apoptosis through autophagy induction.</title><author><name sortKey="Pan, T" sort="Pan, T" uniqKey="Pan T" first="T" last="Pan">T. Pan</name><affiliation wicri:level="2"><nlm:affiliation>Parkinson Disease Research Laboratory, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Parkinson Disease Research Laboratory, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Rawal, P" sort="Rawal, P" uniqKey="Rawal P" first="P" last="Rawal">P. Rawal</name></author><author><name sortKey="Wu, Y" sort="Wu, Y" uniqKey="Wu Y" first="Y" last="Wu">Y. Wu</name></author><author><name sortKey="Xie, W" sort="Xie, W" uniqKey="Xie W" first="W" last="Xie">W. Xie</name></author><author><name sortKey="Jankovic, J" sort="Jankovic, J" uniqKey="Jankovic J" first="J" last="Jankovic">Joseph Jankovic</name><affiliation><country>États-Unis</country><placeName><settlement type="city">Houston</settlement><region type="state">Texas</region></placeName><orgName type="university" n="3">Baylor College of Medicine</orgName></affiliation></author><author><name sortKey="Le, W" sort="Le, W" uniqKey="Le W" first="W" last="Le">W. Le</name></author></analytic><series><title level="j">Neuroscience</title><idno type="e-ISSN">1873-7544</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoptosis (drug effects)</term><term>Apoptosis (physiology)</term><term>Autophagy (drug effects)</term><term>Autophagy (physiology)</term><term>Cell Line, Tumor</term><term>Cytochromes c (metabolism)</term><term>Cytoplasm (drug effects)</term><term>Cytoplasm (physiology)</term><term>Cytoplasm (ultrastructure)</term><term>Electron Transport Complex IV (metabolism)</term><term>Humans</term><term>Insecticides (toxicity)</term><term>Microtubule-Associated Proteins (metabolism)</term><term>Mitochondria (drug effects)</term><term>Mitochondria (physiology)</term><term>Mitochondria (ultrastructure)</term><term>Neuroprotective Agents (pharmacology)</term><term>RNA, Small Interfering (metabolism)</term><term>Rotenone (toxicity)</term><term>Sirolimus (pharmacology)</term><term>Ubiquitinated Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochromes c</term><term>Electron Transport Complex IV</term><term>Microtubule-Associated Proteins</term><term>RNA, Small Interfering</term><term>Ubiquitinated Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term><term>Autophagy</term><term>Cytoplasm</term><term>Mitochondria</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Neuroprotective Agents</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Apoptosis</term><term>Autophagy</term><term>Cytoplasm</term><term>Mitochondria</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Insecticides</term><term>Rotenone</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Cytoplasm</term><term>Mitochondria</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ubiquitin proteasome system (UPS) and autophagy lysosome pathway (ALP) are the two most important routes for degradation of aggregated/misfolded proteins. Additionally, ALP is so far the only known route to clear entire organelles, such as mitochondria. We proposed that enhancement of ALP may be beneficial for some neurodegenerative disorders, such as Parkinson's disease (PD), in which the accumulation of aggregated/misfolded proteins and the dysfunction of mitochondria are the two major pathogenesis. Mitochondrial complex I inhibitor rotenone, which causes dysfunction mitochondria and UPS, has been considered as one of the neurotoxins related to PD. In this study, rotenone-exposed human neuronal SH-SY5Y cells were used as an in vitro model for us to determine whether autophagy enhancer rapamycin could protect against rotenone-induced injury and its underlying mechanisms. The observed results showed that rapamycin alleviated rotenone-induced apoptosis, whose effects were partially blocked when autophagy related gene 5 (Atg5) was suppressed by Atg5 small interference RNA (siRNA) transfection. Additionally, the results showed that rapamycin pretreatment diminished rotenone-induced accumulation of high molecular weight ubiquitinated bands, and reduced rotenone-induced increase of cytochrome c in cytosolic fraction and decreased mitochondrial marker cytochrome oxidase subunit IV (COX IV) in mitochondrial fraction. The changes in cytochrome c and COX IV indicated that the decreased translocation of cytochrome c from mitochondria to cytosol was probably due to the turn over of entire injured mitochondria. The results that lysosome and mitochondria were colocolized within the cells pretreated with rapamycin and that the mitochondria could be found within autophagy double membrane structures further supported that the damaged mitochondria might be cleared through autophagy, which process has been termed as "mitophagy." Our studies suggested that autophagy enhancer rapamycin is neuroprotective against rotenone-induced apoptosis through autophagy enhancement. We concluded that pharmacologically induction of autophagy by rapamycin may represent a useful therapeutic strategy as disease-modifiers in PD.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">19682553</PMID><DateCreated><Year>2009</Year><Month>10</Month><Day>14</Day></DateCreated><DateCompleted><Year>2010</Year><Month>02</Month><Day>12</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-7544</ISSN><JournalIssue CitedMedium="Internet"><Volume>164</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Dec</Month><Day>1</Day></PubDate></JournalIssue><Title>Neuroscience</Title><ISOAbbreviation>Neuroscience</ISOAbbreviation></Journal><ArticleTitle>Rapamycin protects against rotenone-induced apoptosis through autophagy induction.</ArticleTitle><Pagination><MedlinePgn>541-51</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.neuroscience.2009.08.014</ELocationID><Abstract><AbstractText>Ubiquitin proteasome system (UPS) and autophagy lysosome pathway (ALP) are the two most important routes for degradation of aggregated/misfolded proteins. Additionally, ALP is so far the only known route to clear entire organelles, such as mitochondria. We proposed that enhancement of ALP may be beneficial for some neurodegenerative disorders, such as Parkinson's disease (PD), in which the accumulation of aggregated/misfolded proteins and the dysfunction of mitochondria are the two major pathogenesis. Mitochondrial complex I inhibitor rotenone, which causes dysfunction mitochondria and UPS, has been considered as one of the neurotoxins related to PD. In this study, rotenone-exposed human neuronal SH-SY5Y cells were used as an in vitro model for us to determine whether autophagy enhancer rapamycin could protect against rotenone-induced injury and its underlying mechanisms. The observed results showed that rapamycin alleviated rotenone-induced apoptosis, whose effects were partially blocked when autophagy related gene 5 (Atg5) was suppressed by Atg5 small interference RNA (siRNA) transfection. Additionally, the results showed that rapamycin pretreatment diminished rotenone-induced accumulation of high molecular weight ubiquitinated bands, and reduced rotenone-induced increase of cytochrome c in cytosolic fraction and decreased mitochondrial marker cytochrome oxidase subunit IV (COX IV) in mitochondrial fraction. The changes in cytochrome c and COX IV indicated that the decreased translocation of cytochrome c from mitochondria to cytosol was probably due to the turn over of entire injured mitochondria. The results that lysosome and mitochondria were colocolized within the cells pretreated with rapamycin and that the mitochondria could be found within autophagy double membrane structures further supported that the damaged mitochondria might be cleared through autophagy, which process has been termed as "mitophagy." Our studies suggested that autophagy enhancer rapamycin is neuroprotective against rotenone-induced apoptosis through autophagy enhancement. 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Proteins</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>4</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>7</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>8</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2009</Year><Month>8</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>8</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>8</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>2</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">S0306-4522(09)01294-9</ArticleId><ArticleId IdType="doi">10.1016/j.neuroscience.2009.08.014</ArticleId><ArticleId IdType="pubmed">19682553</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Texas</li></region><settlement><li>Houston</li></settlement><orgName><li>Baylor College of Medicine</li></orgName></list><tree><noCountry><name sortKey="Le, W" sort="Le, W" uniqKey="Le W" first="W" last="Le">W. Le</name><name sortKey="Rawal, P" sort="Rawal, P" uniqKey="Rawal P" first="P" last="Rawal">P. Rawal</name><name sortKey="Wu, Y" sort="Wu, Y" uniqKey="Wu Y" first="Y" last="Wu">Y. Wu</name><name sortKey="Xie, W" sort="Xie, W" uniqKey="Xie W" first="W" last="Xie">W. Xie</name></noCountry><country name="États-Unis"><region name="Texas"><name sortKey="Pan, T" sort="Pan, T" uniqKey="Pan T" first="T" last="Pan">T. Pan</name></region><name sortKey="Jankovic, J" sort="Jankovic, J" uniqKey="Jankovic J" first="J" last="Jankovic">Joseph Jankovic</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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