Clinical correlates of mitochondrial function in Huntington's disease muscle.
Identifieur interne : 001C87 ( Ncbi/Merge ); précédent : 001C86; suivant : 001C88Clinical correlates of mitochondrial function in Huntington's disease muscle.
Auteurs : Christopher Turner [Royaume-Uni] ; J Mark Cooper ; Anthony H V. SchapiraSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2007.
English descriptors
- KwdEn :
- Adult, Aged, Case-Control Studies, Electron Transport Complex IV (metabolism), Female, Humans, Huntington Disease (genetics), Huntington Disease (pathology), Huntington Disease (physiopathology), Male, Middle Aged, Mitochondria (physiology), Multienzyme Complexes (metabolism), Muscle, Skeletal (enzymology), Muscle, Skeletal (physiopathology), Muscle, Skeletal (ultrastructure), Nerve Tissue Proteins (genetics), Nuclear Proteins (genetics), Spectrophotometry (methods), Succinate Dehydrogenase (metabolism), Trinucleotide Repeat Expansion (genetics).
- MESH :
- chemical , genetics : Nerve Tissue Proteins, Nuclear Proteins.
- chemical , metabolism : Electron Transport Complex IV, Multienzyme Complexes, Succinate Dehydrogenase.
- enzymology : Muscle, Skeletal.
- genetics : Huntington Disease, Trinucleotide Repeat Expansion.
- methods : Spectrophotometry.
- pathology : Huntington Disease.
- physiology : Mitochondria.
- physiopathology : Huntington Disease, Muscle, Skeletal.
- ultrastructure : Muscle, Skeletal.
- Adult, Aged, Case-Control Studies, Female, Humans, Male, Middle Aged.
Abstract
Huntington's disease (HD) is caused by an abnormally expanded CAG repeat in the IT-15 gene, which encodes a widely expressed protein called huntingtin. Abnormalities of mitochondrial respiratory chain function, specifically complex II/III, have been identified in HD striatum and defects of energy metabolism have been demonstrated in vivo in skeletal muscle in both symptomatic and presymptomatic HD patients. We have investigated respiratory chain function using histochemical and biochemical methods in HD skeletal muscle from 12 patients and compared these with 12 age and sex-matched controls. The data from the HD patients were related to clinical parameters of HD including the Unified Huntington's Disease Rating Scale (UHDRS). There were positive correlations between CAG repeat years (a product of CAG repeat length and age) and both motor (P < 0.002) and cognitive (P < 0.01) scores of the UHDRS. There was no significant difference in the activities of complexes I to IV compared to age-matched controls. However, there were significant correlations for individual HD complex II/III activities with disease duration (P = 0.017), repeat years (P = 0.032), and cognitive scores (P = 0.019). There was also evidence from ultrastructural studies that inclusion formation may occur in HD muscle. These results provide additional evidence that mutant huntingtin influences mitochondrial complex II/III function in non-neuronal tissue (skeletal muscle) and suggest that muscle may be a potential marker of disease progression in HD.
DOI: 10.1002/mds.21540
PubMed: 17557337
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Clinical correlates of mitochondrial function in Huntington's disease muscle.</title><author><name sortKey="Turner, Christopher" sort="Turner, Christopher" uniqKey="Turner C" first="Christopher" last="Turner">Christopher Turner</name><affiliation wicri:level="3"><nlm:affiliation>University Department of Clinical Neurosciences, Royal Free and University College Medical School, University College London, London, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>University Department of Clinical Neurosciences, Royal Free and University College Medical School, University College London, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Cooper, J Mark" sort="Cooper, J Mark" uniqKey="Cooper J" first="J Mark" last="Cooper">J Mark Cooper</name></author><author><name sortKey="Schapira, Anthony H V" sort="Schapira, Anthony H V" uniqKey="Schapira A" first="Anthony H V" last="Schapira">Anthony H V. Schapira</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="doi">10.1002/mds.21540</idno><idno type="RBID">pubmed:17557337</idno><idno type="pmid">17557337</idno><idno type="wicri:Area/PubMed/Corpus">002652</idno><idno type="wicri:Area/PubMed/Curation">002652</idno><idno type="wicri:Area/PubMed/Checkpoint">002914</idno><idno type="wicri:Area/Ncbi/Merge">001C87</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Clinical correlates of mitochondrial function in Huntington's disease muscle.</title><author><name sortKey="Turner, Christopher" sort="Turner, Christopher" uniqKey="Turner C" first="Christopher" last="Turner">Christopher Turner</name><affiliation wicri:level="3"><nlm:affiliation>University Department of Clinical Neurosciences, Royal Free and University College Medical School, University College London, London, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>University Department of Clinical Neurosciences, Royal Free and University College Medical School, University College London, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Cooper, J Mark" sort="Cooper, J Mark" uniqKey="Cooper J" first="J Mark" last="Cooper">J Mark Cooper</name></author><author><name sortKey="Schapira, Anthony H V" sort="Schapira, Anthony H V" uniqKey="Schapira A" first="Anthony H V" last="Schapira">Anthony H V. Schapira</name></author></analytic><series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title><idno type="ISSN">0885-3185</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult</term><term>Aged</term><term>Case-Control Studies</term><term>Electron Transport Complex IV (metabolism)</term><term>Female</term><term>Humans</term><term>Huntington Disease (genetics)</term><term>Huntington Disease (pathology)</term><term>Huntington Disease (physiopathology)</term><term>Male</term><term>Middle Aged</term><term>Mitochondria (physiology)</term><term>Multienzyme Complexes (metabolism)</term><term>Muscle, Skeletal (enzymology)</term><term>Muscle, Skeletal (physiopathology)</term><term>Muscle, Skeletal (ultrastructure)</term><term>Nerve Tissue Proteins (genetics)</term><term>Nuclear Proteins (genetics)</term><term>Spectrophotometry (methods)</term><term>Succinate Dehydrogenase (metabolism)</term><term>Trinucleotide Repeat Expansion (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nerve Tissue Proteins</term><term>Nuclear Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Electron Transport Complex IV</term><term>Multienzyme Complexes</term><term>Succinate Dehydrogenase</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Muscle, Skeletal</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Huntington Disease</term><term>Trinucleotide Repeat Expansion</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Spectrophotometry</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Huntington Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Huntington Disease</term><term>Muscle, Skeletal</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Muscle, Skeletal</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Aged</term><term>Case-Control Studies</term><term>Female</term><term>Humans</term><term>Male</term><term>Middle Aged</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Huntington's disease (HD) is caused by an abnormally expanded CAG repeat in the IT-15 gene, which encodes a widely expressed protein called huntingtin. Abnormalities of mitochondrial respiratory chain function, specifically complex II/III, have been identified in HD striatum and defects of energy metabolism have been demonstrated in vivo in skeletal muscle in both symptomatic and presymptomatic HD patients. We have investigated respiratory chain function using histochemical and biochemical methods in HD skeletal muscle from 12 patients and compared these with 12 age and sex-matched controls. The data from the HD patients were related to clinical parameters of HD including the Unified Huntington's Disease Rating Scale (UHDRS). There were positive correlations between CAG repeat years (a product of CAG repeat length and age) and both motor (P < 0.002) and cognitive (P < 0.01) scores of the UHDRS. There was no significant difference in the activities of complexes I to IV compared to age-matched controls. However, there were significant correlations for individual HD complex II/III activities with disease duration (P = 0.017), repeat years (P = 0.032), and cognitive scores (P = 0.019). There was also evidence from ultrastructural studies that inclusion formation may occur in HD muscle. These results provide additional evidence that mutant huntingtin influences mitochondrial complex II/III function in non-neuronal tissue (skeletal muscle) and suggest that muscle may be a potential marker of disease progression in HD.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">17557337</PMID><DateCreated><Year>2007</Year><Month>10</Month><Day>01</Day></DateCreated><DateCompleted><Year>2008</Year><Month>01</Month><Day>09</Day></DateCompleted><DateRevised><Year>2012</Year><Month>07</Month><Day>11</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0885-3185</ISSN><JournalIssue CitedMedium="Print"><Volume>22</Volume><Issue>12</Issue><PubDate><Year>2007</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>Movement disorders : official journal of the Movement Disorder Society</Title><ISOAbbreviation>Mov. Disord.</ISOAbbreviation></Journal><ArticleTitle>Clinical correlates of mitochondrial function in Huntington's disease muscle.</ArticleTitle><Pagination><MedlinePgn>1715-21</MedlinePgn></Pagination><Abstract><AbstractText>Huntington's disease (HD) is caused by an abnormally expanded CAG repeat in the IT-15 gene, which encodes a widely expressed protein called huntingtin. Abnormalities of mitochondrial respiratory chain function, specifically complex II/III, have been identified in HD striatum and defects of energy metabolism have been demonstrated in vivo in skeletal muscle in both symptomatic and presymptomatic HD patients. We have investigated respiratory chain function using histochemical and biochemical methods in HD skeletal muscle from 12 patients and compared these with 12 age and sex-matched controls. The data from the HD patients were related to clinical parameters of HD including the Unified Huntington's Disease Rating Scale (UHDRS). There were positive correlations between CAG repeat years (a product of CAG repeat length and age) and both motor (P < 0.002) and cognitive (P < 0.01) scores of the UHDRS. There was no significant difference in the activities of complexes I to IV compared to age-matched controls. However, there were significant correlations for individual HD complex II/III activities with disease duration (P = 0.017), repeat years (P = 0.032), and cognitive scores (P = 0.019). There was also evidence from ultrastructural studies that inclusion formation may occur in HD muscle. These results provide additional evidence that mutant huntingtin influences mitochondrial complex II/III function in non-neuronal tissue (skeletal muscle) and suggest that muscle may be a potential marker of disease progression in HD.</AbstractText><CopyrightInformation>(c) 2007 Movement Disorder Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>Christopher</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>University Department of Clinical Neurosciences, Royal Free and University College Medical School, University College London, London, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cooper</LastName><ForeName>J Mark</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Schapira</LastName><ForeName>Anthony H V</ForeName><Initials>AH</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mov Disord</MedlineTA><NlmUniqueID>8610688</NlmUniqueID><ISSNLinking>0885-3185</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C086055">HTT protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009419">Nerve Tissue Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009687">Nuclear Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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Skeletal</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000503">physiopathology</QualifierName><QualifierName MajorTopicYN="N" UI="Q000648">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D009419">Nerve Tissue Proteins</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D009687">Nuclear Proteins</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D013053">Spectrophotometry</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000379">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D013385">Succinate Dehydrogenase</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D019680">Trinucleotide Repeat Expansion</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>6</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>1</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>6</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1002/mds.21540</ArticleId><ArticleId IdType="pubmed">17557337</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement></list><tree><noCountry><name sortKey="Cooper, J Mark" sort="Cooper, J Mark" uniqKey="Cooper J" first="J Mark" last="Cooper">J Mark Cooper</name><name sortKey="Schapira, Anthony H V" sort="Schapira, Anthony H V" uniqKey="Schapira A" first="Anthony H V" last="Schapira">Anthony H V. Schapira</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Turner, Christopher" sort="Turner, Christopher" uniqKey="Turner C" first="Christopher" last="Turner">Christopher Turner</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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