Identification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson's disease.
Identifieur interne : 000B93 ( PubMed/Checkpoint ); précédent : 000B92; suivant : 000B94Identification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson's disease.
Auteurs : Juliane Proft [Canada] ; Jamshid Faraji ; Jerrah C. Robbins ; Fabiola C R. Zucchi ; Xiaoxi Zhao ; Gerlinde A. Metz ; Janice E A. BraunSource :
- PloS one [ 1932-6203 ] ; 2011.
English descriptors
- KwdEn :
- 1-Methyl-4-phenylpyridinium (pharmacology), Animals, Cell Line, Tumor, Disease Models, Animal, Female, Gene Expression Regulation (drug effects), HSP40 Heat-Shock Proteins (chemistry), HSP40 Heat-Shock Proteins (metabolism), Homeostasis (drug effects), Mice, Mitochondria (drug effects), Mitochondria (metabolism), Molecular Weight, Oxidopamine (pharmacology), Parkinson Disease (etiology), Parkinson Disease (metabolism), Parkinson Disease (pathology), Parkinson Disease (physiopathology), Psychomotor Performance (drug effects), Rats, Rats, Long-Evans, Signal Transduction (drug effects), alpha-Synuclein (metabolism).
- MESH :
- chemical , chemistry : HSP40 Heat-Shock Proteins.
- chemical , metabolism : HSP40 Heat-Shock Proteins, alpha-Synuclein.
- chemical , pharmacology : 1-Methyl-4-phenylpyridinium, Oxidopamine.
- drug effects : Gene Expression Regulation, Homeostasis, Mitochondria, Psychomotor Performance, Signal Transduction.
- etiology : Parkinson Disease.
- metabolism : Mitochondria, Parkinson Disease.
- pathology : Parkinson Disease.
- physiopathology : Parkinson Disease.
- Animals, Cell Line, Tumor, Disease Models, Animal, Female, Mice, Molecular Weight, Rats, Rats, Long-Evans.
Abstract
Parkinson's disease (PD) is a common neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra and the aggregation of α-synuclein into Lewy bodies. Existing therapies address motor dysfunction but do not halt progression of the disease. A still unresolved question is the biochemical pathway that modulates the outcome of protein misfolding and aggregation processes in PD. The molecular chaperone network plays an important defensive role against cellular protein misfolding and has been identified as protective in experimental models of protein misfolding diseases like PD. Molecular mechanisms underlying chaperone-neuroprotection are actively under investigation. Current evidence implicates a number of molecular chaperones in PD including Hsp25, Hsp70 and Hsp90, however their precise involvement in the neurodegenerative cascade is unresolved. The J protein family (DnaJ or Hsp40 protein family) has long been known to be important in protein conformational processes.We assessed sensory and motor function of control and PD rats and then evaluated the brain region-specific expression levels of select J proteins by Western analysis. Surprisingly, we observed a widespread 26 kDa breakdown product of the J protein, TID1, (tumorous imaginal discs, mtHsp40 or DnaJ3) in a 6-hydroxydopamine (6-OHDA) rat model of PD in which food handling, gait symmetry and sensory performance were impaired. Greater behavioral deficits were associated with lower TID1 expression. Furthermore, direct application of either 6-OHDA or MPP+ (1-methyl-4-phenylpyridinum) to CAD (CNS-derived catecholinaminergic neuronal cell line) cell cultures, reduced TID1 expression levels.Our results suggest that changes in cellular TID1 are a factor in the pathogenesis of PD by impeding functional and structural compensation and exaggerating neurodegenerative processes. In contrast, no changes were observed in CSPα, Hsp40, Hsp70, Hsc70 and PrP(C) levels and no activation of caspase3 was observed. This study links TID1 to PD and provides a new target for therapeutics that halts the PD progression.
DOI: 10.1371/journal.pone.0026045
PubMed: 22016808
Affiliations:
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pubmed:22016808Le document en format XML
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Robbins</name></author><author><name sortKey="Zucchi, Fabiola C R" sort="Zucchi, Fabiola C R" uniqKey="Zucchi F" first="Fabiola C R" last="Zucchi">Fabiola C R. Zucchi</name></author><author><name sortKey="Zhao, Xiaoxi" sort="Zhao, Xiaoxi" uniqKey="Zhao X" first="Xiaoxi" last="Zhao">Xiaoxi Zhao</name></author><author><name sortKey="Metz, Gerlinde A" sort="Metz, Gerlinde A" uniqKey="Metz G" first="Gerlinde A" last="Metz">Gerlinde A. Metz</name></author><author><name sortKey="Braun, Janice E A" sort="Braun, Janice E A" uniqKey="Braun J" first="Janice E A" last="Braun">Janice E A. 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Existing therapies address motor dysfunction but do not halt progression of the disease. A still unresolved question is the biochemical pathway that modulates the outcome of protein misfolding and aggregation processes in PD. The molecular chaperone network plays an important defensive role against cellular protein misfolding and has been identified as protective in experimental models of protein misfolding diseases like PD. Molecular mechanisms underlying chaperone-neuroprotection are actively under investigation. Current evidence implicates a number of molecular chaperones in PD including Hsp25, Hsp70 and Hsp90, however their precise involvement in the neurodegenerative cascade is unresolved. The J protein family (DnaJ or Hsp40 protein family) has long been known to be important in protein conformational processes.We assessed sensory and motor function of control and PD rats and then evaluated the brain region-specific expression levels of select J proteins by Western analysis. Surprisingly, we observed a widespread 26 kDa breakdown product of the J protein, TID1, (tumorous imaginal discs, mtHsp40 or DnaJ3) in a 6-hydroxydopamine (6-OHDA) rat model of PD in which food handling, gait symmetry and sensory performance were impaired. Greater behavioral deficits were associated with lower TID1 expression. Furthermore, direct application of either 6-OHDA or MPP+ (1-methyl-4-phenylpyridinum) to CAD (CNS-derived catecholinaminergic neuronal cell line) cell cultures, reduced TID1 expression levels.Our results suggest that changes in cellular TID1 are a factor in the pathogenesis of PD by impeding functional and structural compensation and exaggerating neurodegenerative processes. In contrast, no changes were observed in CSPα, Hsp40, Hsp70, Hsc70 and PrP(C) levels and no activation of caspase3 was observed. This study links TID1 to PD and provides a new target for therapeutics that halts the PD progression.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22016808</PMID><DateCreated><Year>2011</Year><Month>10</Month><Day>21</Day></DateCreated><DateCompleted><Year>2012</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>10</Issue><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Identification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>e26045</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0026045</ELocationID><Abstract><AbstractText>Parkinson's disease (PD) is a common neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra and the aggregation of α-synuclein into Lewy bodies. Existing therapies address motor dysfunction but do not halt progression of the disease. A still unresolved question is the biochemical pathway that modulates the outcome of protein misfolding and aggregation processes in PD. The molecular chaperone network plays an important defensive role against cellular protein misfolding and has been identified as protective in experimental models of protein misfolding diseases like PD. Molecular mechanisms underlying chaperone-neuroprotection are actively under investigation. Current evidence implicates a number of molecular chaperones in PD including Hsp25, Hsp70 and Hsp90, however their precise involvement in the neurodegenerative cascade is unresolved. The J protein family (DnaJ or Hsp40 protein family) has long been known to be important in protein conformational processes.We assessed sensory and motor function of control and PD rats and then evaluated the brain region-specific expression levels of select J proteins by Western analysis. Surprisingly, we observed a widespread 26 kDa breakdown product of the J protein, TID1, (tumorous imaginal discs, mtHsp40 or DnaJ3) in a 6-hydroxydopamine (6-OHDA) rat model of PD in which food handling, gait symmetry and sensory performance were impaired. Greater behavioral deficits were associated with lower TID1 expression. Furthermore, direct application of either 6-OHDA or MPP+ (1-methyl-4-phenylpyridinum) to CAD (CNS-derived catecholinaminergic neuronal cell line) cell cultures, reduced TID1 expression levels.Our results suggest that changes in cellular TID1 are a factor in the pathogenesis of PD by impeding functional and structural compensation and exaggerating neurodegenerative processes. In contrast, no changes were observed in CSPα, Hsp40, Hsp70, Hsc70 and PrP(C) levels and no activation of caspase3 was observed. This study links TID1 to PD and provides a new target for therapeutics that halts the PD progression.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Proft</LastName><ForeName>Juliane</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Hotchkiss Brain Institute, Department of Physiology and Pharmacology, University of Calgary, Calgary, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Faraji</LastName><ForeName>Jamshid</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Robbins</LastName><ForeName>Jerrah C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Zucchi</LastName><ForeName>Fabiola C R</ForeName><Initials>FC</Initials></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Xiaoxi</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Metz</LastName><ForeName>Gerlinde A</ForeName><Initials>GA</Initials></Author><Author ValidYN="Y"><LastName>Braun</LastName><ForeName>Janice E A</ForeName><Initials>JE</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R21 NS043588</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>MOP74713</GrantID><Agency>Canadian Institutes of Health Research</Agency><Country>Canada</Country></Grant><Grant><GrantID>NS043588</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>10</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050956">HSP40 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>8HW4YBZ748</RegistryNumber><NameOfSubstance UI="D016627">Oxidopamine</NameOfSubstance></Chemical><Chemical><RegistryNumber>R865A5OY8J</RegistryNumber><NameOfSubstance UI="D015655">1-Methyl-4-phenylpyridinium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2001 Apr 20;276(16):13087-95</RefSource><PMID Version="1">11116152</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2010;5(4):e10014</RefSource><PMID 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MajorTopicYN="N">Oxidopamine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011597" MajorTopicYN="N">Psychomotor Performance</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020318" MajorTopicYN="N">Rats, Long-Evans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC3189242</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>07</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>10</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>10</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>2</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22016808</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0026045</ArticleId><ArticleId IdType="pii">PONE-D-11-13403</ArticleId><ArticleId IdType="pmc">PMC3189242</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Alberta</li></region><settlement><li>Calgary</li></settlement><orgName><li>Université de Calgary</li></orgName></list><tree><noCountry><name sortKey="Braun, Janice E A" sort="Braun, Janice E A" uniqKey="Braun J" first="Janice E A" last="Braun">Janice E A. Braun</name><name sortKey="Faraji, Jamshid" sort="Faraji, Jamshid" uniqKey="Faraji J" first="Jamshid" last="Faraji">Jamshid Faraji</name><name sortKey="Metz, Gerlinde A" sort="Metz, Gerlinde A" uniqKey="Metz G" first="Gerlinde A" last="Metz">Gerlinde A. Metz</name><name sortKey="Robbins, Jerrah C" sort="Robbins, Jerrah C" uniqKey="Robbins J" first="Jerrah C" last="Robbins">Jerrah C. Robbins</name><name sortKey="Zhao, Xiaoxi" sort="Zhao, Xiaoxi" uniqKey="Zhao X" first="Xiaoxi" last="Zhao">Xiaoxi Zhao</name><name sortKey="Zucchi, Fabiola C R" sort="Zucchi, Fabiola C R" uniqKey="Zucchi F" first="Fabiola C R" last="Zucchi">Fabiola C R. Zucchi</name></noCountry><country name="Canada"><region name="Alberta"><name sortKey="Proft, Juliane" sort="Proft, Juliane" uniqKey="Proft J" first="Juliane" last="Proft">Juliane Proft</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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