Oxidative stress alters the regulatory control of p66Shc and Akt in PINK1 deficient cells.
Identifieur interne : 000D00 ( Ncbi/Merge ); précédent : 000C99; suivant : 000D01Oxidative stress alters the regulatory control of p66Shc and Akt in PINK1 deficient cells.
Auteurs : Mary C. Maj [Canada] ; Ilona Tkachyova ; Pratik Patel ; Jane B. Addis ; Nevena Mackay ; Valeriy Levandovskiy ; Jisoo Lee ; Anthony E. Lang ; Jessie M. Cameron ; Brian H. RobinsonSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.
English descriptors
- KwdEn :
- Cell Line, Fibroblasts (metabolism), Glutathione Peroxidase (metabolism), Humans, Oxidative Stress, Parkinson Disease (metabolism), Peroxiredoxins (metabolism), Phosphorylation, Protein Kinases (genetics), Protein Kinases (metabolism), Proto-Oncogene Proteins c-akt (metabolism), Reactive Oxygen Species (metabolism), Serine (metabolism), Shc Signaling Adaptor Proteins (metabolism), Src Homology 2 Domain-Containing, Transforming Protein 1, Superoxide Dismutase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , genetics : Protein Kinases.
- chemical , metabolism : Glutathione Peroxidase, Peroxiredoxins, Protein Kinases, Proto-Oncogene Proteins c-akt, Reactive Oxygen Species, Serine, Shc Signaling Adaptor Proteins, Superoxide Dismutase, Thioredoxins.
- metabolism : Fibroblasts, Parkinson Disease.
- Cell Line, Humans, Oxidative Stress, Phosphorylation, Src Homology 2 Domain-Containing, Transforming Protein 1.
Abstract
Mitochondrial dysfunction is involved in the underlying pathology of Parkinson's Disease (PD). PINK1 deficiency, which gives rise to familial early-onset PD, is associated with this dysfunction as well as increased oxidative stress. We have established primary fibroblast cell lines from two patients with PD who carry mutations in the PINK1 gene. The phosphorylation of Akt is abrogated in the presence of oxidative stressors in the complete absence of PINK1 suggesting enhanced apoptotic signalling. We have found an imbalance between the production of reactive oxygen species where the capacity of the cell to remove these toxins by anti-oxidative enzymes is greatly reduced. The expression levels of the anti-oxidant enzymes glutathione peroxidase-1, MnSOD, peroxiredoxin-3 and thioredoxin-2 were diminished. The p66(Shc) adaptor protein has recently been identified to become activated by oxidative stress by phosphorylation at residue Ser36 which then translocates to the mitochondrial inner membrane space. The phosphorylation of p66(Shc) at Ser36 is significantly increased in PINK1 deficient cell lines under normal tissue culture conditions, further still in the presence of compounds which elicit oxidative stress. The stable transfection of PINK1 in the fibroblasts which display the null phenotype ameliorates the hyper-phosphorylation of p66(Shc).
DOI: 10.1016/j.bbrc.2010.07.033
PubMed: 20637729
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Maj</name><affiliation wicri:level="1"><nlm:affiliation>Metabolism Research Programme, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8.</nlm:affiliation><country>Canada</country><wicri:regionArea>Metabolism Research Programme, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON</wicri:regionArea><wicri:noRegion>ON</wicri:noRegion></affiliation></author><author><name sortKey="Tkachyova, Ilona" sort="Tkachyova, Ilona" uniqKey="Tkachyova I" first="Ilona" last="Tkachyova">Ilona Tkachyova</name></author><author><name sortKey="Patel, Pratik" sort="Patel, Pratik" uniqKey="Patel P" first="Pratik" last="Patel">Pratik Patel</name></author><author><name sortKey="Addis, Jane B" sort="Addis, Jane B" uniqKey="Addis J" first="Jane B" last="Addis">Jane B. Addis</name></author><author><name sortKey="Mackay, Nevena" sort="Mackay, Nevena" uniqKey="Mackay N" first="Nevena" last="Mackay">Nevena Mackay</name></author><author><name sortKey="Levandovskiy, Valeriy" sort="Levandovskiy, Valeriy" uniqKey="Levandovskiy V" first="Valeriy" last="Levandovskiy">Valeriy Levandovskiy</name></author><author><name sortKey="Lee, Jisoo" sort="Lee, Jisoo" uniqKey="Lee J" first="Jisoo" last="Lee">Jisoo Lee</name></author><author><name sortKey="Lang, Anthony E" sort="Lang, Anthony E" uniqKey="Lang A" first="Anthony E" last="Lang">Anthony E. Lang</name></author><author><name sortKey="Cameron, Jessie M" sort="Cameron, Jessie M" uniqKey="Cameron J" first="Jessie M" last="Cameron">Jessie M. Cameron</name></author><author><name sortKey="Robinson, Brian H" sort="Robinson, Brian H" uniqKey="Robinson B" first="Brian H" last="Robinson">Brian H. 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Maj</name><affiliation wicri:level="1"><nlm:affiliation>Metabolism Research Programme, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8.</nlm:affiliation><country>Canada</country><wicri:regionArea>Metabolism Research Programme, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON</wicri:regionArea><wicri:noRegion>ON</wicri:noRegion></affiliation></author><author><name sortKey="Tkachyova, Ilona" sort="Tkachyova, Ilona" uniqKey="Tkachyova I" first="Ilona" last="Tkachyova">Ilona Tkachyova</name></author><author><name sortKey="Patel, Pratik" sort="Patel, Pratik" uniqKey="Patel P" first="Pratik" last="Patel">Pratik Patel</name></author><author><name sortKey="Addis, Jane B" sort="Addis, Jane B" uniqKey="Addis J" first="Jane B" last="Addis">Jane B. Addis</name></author><author><name sortKey="Mackay, Nevena" sort="Mackay, Nevena" uniqKey="Mackay N" first="Nevena" last="Mackay">Nevena Mackay</name></author><author><name sortKey="Levandovskiy, Valeriy" sort="Levandovskiy, Valeriy" uniqKey="Levandovskiy V" first="Valeriy" last="Levandovskiy">Valeriy Levandovskiy</name></author><author><name sortKey="Lee, Jisoo" sort="Lee, Jisoo" uniqKey="Lee J" first="Jisoo" last="Lee">Jisoo Lee</name></author><author><name sortKey="Lang, Anthony E" sort="Lang, Anthony E" uniqKey="Lang A" first="Anthony E" last="Lang">Anthony E. Lang</name></author><author><name sortKey="Cameron, Jessie M" sort="Cameron, Jessie M" uniqKey="Cameron J" first="Jessie M" last="Cameron">Jessie M. Cameron</name></author><author><name sortKey="Robinson, Brian H" sort="Robinson, Brian H" uniqKey="Robinson B" first="Brian H" last="Robinson">Brian H. Robinson</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Fibroblasts (metabolism)</term><term>Glutathione Peroxidase (metabolism)</term><term>Humans</term><term>Oxidative Stress</term><term>Parkinson Disease (metabolism)</term><term>Peroxiredoxins (metabolism)</term><term>Phosphorylation</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Proto-Oncogene Proteins c-akt (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>Serine (metabolism)</term><term>Shc Signaling Adaptor Proteins (metabolism)</term><term>Src Homology 2 Domain-Containing, Transforming Protein 1</term><term>Superoxide Dismutase (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Peroxidase</term><term>Peroxiredoxins</term><term>Protein Kinases</term><term>Proto-Oncogene Proteins c-akt</term><term>Reactive Oxygen Species</term><term>Serine</term><term>Shc Signaling Adaptor Proteins</term><term>Superoxide Dismutase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fibroblasts</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Oxidative Stress</term><term>Phosphorylation</term><term>Src Homology 2 Domain-Containing, Transforming Protein 1</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mitochondrial dysfunction is involved in the underlying pathology of Parkinson's Disease (PD). PINK1 deficiency, which gives rise to familial early-onset PD, is associated with this dysfunction as well as increased oxidative stress. We have established primary fibroblast cell lines from two patients with PD who carry mutations in the PINK1 gene. The phosphorylation of Akt is abrogated in the presence of oxidative stressors in the complete absence of PINK1 suggesting enhanced apoptotic signalling. We have found an imbalance between the production of reactive oxygen species where the capacity of the cell to remove these toxins by anti-oxidative enzymes is greatly reduced. The expression levels of the anti-oxidant enzymes glutathione peroxidase-1, MnSOD, peroxiredoxin-3 and thioredoxin-2 were diminished. The p66(Shc) adaptor protein has recently been identified to become activated by oxidative stress by phosphorylation at residue Ser36 which then translocates to the mitochondrial inner membrane space. The phosphorylation of p66(Shc) at Ser36 is significantly increased in PINK1 deficient cell lines under normal tissue culture conditions, further still in the presence of compounds which elicit oxidative stress. The stable transfection of PINK1 in the fibroblasts which display the null phenotype ameliorates the hyper-phosphorylation of p66(Shc).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20637729</PMID><DateCreated><Year>2010</Year><Month>08</Month><Day>30</Day></DateCreated><DateCompleted><Year>2010</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>399</Volume><Issue>3</Issue><PubDate><Year>2010</Year><Month>Aug</Month><Day>27</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Oxidative stress alters the regulatory control of p66Shc and Akt in PINK1 deficient cells.</ArticleTitle><Pagination><MedlinePgn>331-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2010.07.033</ELocationID><Abstract><AbstractText>Mitochondrial dysfunction is involved in the underlying pathology of Parkinson's Disease (PD). PINK1 deficiency, which gives rise to familial early-onset PD, is associated with this dysfunction as well as increased oxidative stress. We have established primary fibroblast cell lines from two patients with PD who carry mutations in the PINK1 gene. The phosphorylation of Akt is abrogated in the presence of oxidative stressors in the complete absence of PINK1 suggesting enhanced apoptotic signalling. We have found an imbalance between the production of reactive oxygen species where the capacity of the cell to remove these toxins by anti-oxidative enzymes is greatly reduced. The expression levels of the anti-oxidant enzymes glutathione peroxidase-1, MnSOD, peroxiredoxin-3 and thioredoxin-2 were diminished. The p66(Shc) adaptor protein has recently been identified to become activated by oxidative stress by phosphorylation at residue Ser36 which then translocates to the mitochondrial inner membrane space. The phosphorylation of p66(Shc) at Ser36 is significantly increased in PINK1 deficient cell lines under normal tissue culture conditions, further still in the presence of compounds which elicit oxidative stress. The stable transfection of PINK1 in the fibroblasts which display the null phenotype ameliorates the hyper-phosphorylation of p66(Shc).</AbstractText><CopyrightInformation>Copyright 2010 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maj</LastName><ForeName>Mary C</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>Metabolism Research Programme, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tkachyova</LastName><ForeName>Ilona</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Patel</LastName><ForeName>Pratik</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Addis</LastName><ForeName>Jane B</ForeName><Initials>JB</Initials></Author><Author ValidYN="Y"><LastName>Mackay</LastName><ForeName>Nevena</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Levandovskiy</LastName><ForeName>Valeriy</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Jisoo</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Lang</LastName><ForeName>Anthony E</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Cameron</LastName><ForeName>Jessie M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Robinson</LastName><ForeName>Brian H</ForeName><Initials>BH</Initials></Author></AuthorList><Language>eng</Language><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>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C528024">SHC1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D055765">Shc Signaling Adaptor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000071425">Src Homology 2 Domain-Containing, Transforming Protein 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>452VLY9402</RegistryNumber><NameOfSubstance UI="D012694">Serine</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C117216">glutathione peroxidase GPX1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.15.1.1</RegistryNumber><NameOfSubstance UI="D013482">Superoxide Dismutase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C433927">PTEN-induced putative kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D051057">Proto-Oncogene Proteins c-akt</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005347" MajorTopicYN="N">Fibroblasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051057" MajorTopicYN="N">Proto-Oncogene Proteins c-akt</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055765" MajorTopicYN="N">Shc Signaling Adaptor Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000071425" MajorTopicYN="N">Src Homology 2 Domain-Containing, Transforming Protein 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013482" MajorTopicYN="N">Superoxide Dismutase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>06</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>07</Month><Day>12</Day></PubMedPubDate><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>2010</Year><Month>9</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20637729</ArticleId><ArticleId IdType="pii">S0006-291X(10)01335-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2010.07.033</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Addis, Jane B" sort="Addis, Jane B" uniqKey="Addis J" first="Jane B" last="Addis">Jane B. Addis</name><name sortKey="Cameron, Jessie M" sort="Cameron, Jessie M" uniqKey="Cameron J" first="Jessie M" last="Cameron">Jessie M. Cameron</name><name sortKey="Lang, Anthony E" sort="Lang, Anthony E" uniqKey="Lang A" first="Anthony E" last="Lang">Anthony E. Lang</name><name sortKey="Lee, Jisoo" sort="Lee, Jisoo" uniqKey="Lee J" first="Jisoo" last="Lee">Jisoo Lee</name><name sortKey="Levandovskiy, Valeriy" sort="Levandovskiy, Valeriy" uniqKey="Levandovskiy V" first="Valeriy" last="Levandovskiy">Valeriy Levandovskiy</name><name sortKey="Mackay, Nevena" sort="Mackay, Nevena" uniqKey="Mackay N" first="Nevena" last="Mackay">Nevena Mackay</name><name sortKey="Patel, Pratik" sort="Patel, Pratik" uniqKey="Patel P" first="Pratik" last="Patel">Pratik Patel</name><name sortKey="Robinson, Brian H" sort="Robinson, Brian H" uniqKey="Robinson B" first="Brian H" last="Robinson">Brian H. Robinson</name><name sortKey="Tkachyova, Ilona" sort="Tkachyova, Ilona" uniqKey="Tkachyova I" first="Ilona" last="Tkachyova">Ilona Tkachyova</name></noCountry><country name="Canada"><noRegion><name sortKey="Maj, Mary C" sort="Maj, Mary C" uniqKey="Maj M" first="Mary C" last="Maj">Mary C. Maj</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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