TorsinA immunoreactivity in inclusion bodies in trinucleotide repeat diseases
Identifieur interne : 003F12 ( Main/Exploration ); précédent : 003F11; suivant : 003F13TorsinA immunoreactivity in inclusion bodies in trinucleotide repeat diseases
Auteurs : Ruth H. Walker [États-Unis] ; Paul F. Good [États-Unis] ; P. Shashidharan [États-Unis]Source :
- Movement Disorders [ 0885-3185 ] ; 2003-09.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Homme.
English descriptors
- KwdEn :
- Antibodies (metabolism), Brain (metabolism), Carrier Proteins (metabolism), Exploration, Fluorescence, Human, Humans, Huntington Disease (genetics), Huntington Disease (metabolism), Huntington disease, Immunohistochemistry, Inclusion Bodies (metabolism), Inclusion body, Machado-Joseph Disease (genetics), Machado-Joseph Disease (metabolism), Molecular Chaperones, Neurons (metabolism), Repeated sequence, Spinocerebellar ataxia, Trinucleotide, Trinucleotide Repeats, inclusion bodies, torsinA, trinucleotide repeats.
- MESH :
- chemical , metabolism : Antibodies, Carrier Proteins.
- genetics : Huntington Disease, Machado-Joseph Disease.
- metabolism : Brain, Huntington Disease, Inclusion Bodies, Machado-Joseph Disease, Neurons.
- Fluorescence, Humans, Immunohistochemistry, Molecular Chaperones, Trinucleotide Repeats.
Abstract
A mutation of the DYT1 gene, which codes for torsinA, has been identified as a cause of autosomal dominantly inherited dystonia. The function of torsinA is not yet known, but it is found throughout the central nervous system and has been identified in Lewy bodies in Parkinson's disease. We examined cases of Huntington's disease, spinocerebellar ataxia type III, and Huntington's disease‐like 2 using antibodies to torsinA, and found that ubiquitinated, intranuclear neuronal inclusions were torsinA‐immunoreactive, possibly indicating a role for torsinA in protein degradation. © 2003 Movement Disorder Society
Url:
DOI: 10.1002/mds.10487
Affiliations:
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Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2003-09">2003-09</date><biblScope unit="vol">18</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1041">1041</biblScope><biblScope unit="page" to="1044">1044</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">7432A7592CDF04107CD367B658DE0B27232BAD12</idno><idno type="DOI">10.1002/mds.10487</idno><idno type="ArticleID">MDS10487</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies (metabolism)</term><term>Brain (metabolism)</term><term>Carrier Proteins (metabolism)</term><term>Exploration</term><term>Fluorescence</term><term>Human</term><term>Humans</term><term>Huntington Disease (genetics)</term><term>Huntington Disease (metabolism)</term><term>Huntington disease</term><term>Immunohistochemistry</term><term>Inclusion Bodies (metabolism)</term><term>Inclusion body</term><term>Machado-Joseph Disease (genetics)</term><term>Machado-Joseph Disease (metabolism)</term><term>Molecular Chaperones</term><term>Neurons (metabolism)</term><term>Repeated sequence</term><term>Spinocerebellar ataxia</term><term>Trinucleotide</term><term>Trinucleotide Repeats</term><term>inclusion bodies</term><term>torsinA</term><term>trinucleotide repeats</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies</term><term>Carrier Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Huntington Disease</term><term>Machado-Joseph Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Huntington Disease</term><term>Inclusion Bodies</term><term>Machado-Joseph Disease</term><term>Neurons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Fluorescence</term><term>Humans</term><term>Immunohistochemistry</term><term>Molecular Chaperones</term><term>Trinucleotide Repeats</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Ataxie spinocérébelleuse</term><term>Chorée Huntington</term><term>Corps inclusion</term><term>Exploration</term><term>Homme</term><term>Immunohistochimie</term><term>Séquence répétée</term><term>TorsinA</term><term>Trinucléotide</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A mutation of the DYT1 gene, which codes for torsinA, has been identified as a cause of autosomal dominantly inherited dystonia. The function of torsinA is not yet known, but it is found throughout the central nervous system and has been identified in Lewy bodies in Parkinson's disease. We examined cases of Huntington's disease, spinocerebellar ataxia type III, and Huntington's disease‐like 2 using antibodies to torsinA, and found that ubiquitinated, intranuclear neuronal inclusions were torsinA‐immunoreactive, possibly indicating a role for torsinA in protein degradation. © 2003 Movement Disorder Society</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Walker, Ruth H" sort="Walker, Ruth H" uniqKey="Walker R" first="Ruth H." last="Walker">Ruth H. Walker</name></region><name sortKey="Good, Paul F" sort="Good, Paul F" uniqKey="Good P" first="Paul F." last="Good">Paul F. Good</name><name sortKey="Shashidharan, P" sort="Shashidharan, P" uniqKey="Shashidharan P" first="P." last="Shashidharan">P. Shashidharan</name><name sortKey="Walker, Ruth H" sort="Walker, Ruth H" uniqKey="Walker R" first="Ruth H." last="Walker">Ruth H. Walker</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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