Ubiquitin–proteasome system and Parkinson's disease
Identifieur interne : 003138 ( Main/Exploration ); précédent : 003137; suivant : 003139Ubiquitin–proteasome system and Parkinson's disease
Auteurs : C. Warren Olanow [États-Unis] ; Kevin St. P. Mcnaught [États-Unis]Source :
- Movement Disorders [ 0885-3185 ] ; 2006-11.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Age Factors, Animals, Central Nervous System (metabolism), Humans, Models, Biological, Multicatalytic endopeptidase complex, Mutation, Nervous system diseases, Parkinson Disease (genetics), Parkinson Disease (metabolism), Parkinson disease, Parkinson's disease, Proteasome Endopeptidase Complex (genetics), Proteasome Endopeptidase Complex (metabolism), Protein, Ubiquitin, Ubiquitin (genetics), Ubiquitin (metabolism), alpha‐synuclein, proteasome, protein accumulation, ubiquitin.
- MESH :
- chemical , genetics : Proteasome Endopeptidase Complex, Ubiquitin.
- genetics : Parkinson Disease.
- metabolism : Central Nervous System, Parkinson Disease, Proteasome Endopeptidase Complex, Ubiquitin.
- Age Factors, Animals, Humans, Models, Biological, Mutation.
Abstract
Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society
Url:
DOI: 10.1002/mds.21013
Affiliations:
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Le document en format XML
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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="2006-11">2006-11</date><biblScope unit="vol">21</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="1806">1806</biblScope><biblScope unit="page" to="1823">1823</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</idno><idno type="DOI">10.1002/mds.21013</idno><idno type="ArticleID">MDS21013</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Age Factors</term><term>Animals</term><term>Central Nervous System (metabolism)</term><term>Humans</term><term>Models, Biological</term><term>Multicatalytic endopeptidase complex</term><term>Mutation</term><term>Nervous system diseases</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson disease</term><term>Parkinson's disease</term><term>Proteasome Endopeptidase Complex (genetics)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Protein</term><term>Ubiquitin</term><term>Ubiquitin (genetics)</term><term>Ubiquitin (metabolism)</term><term>alpha‐synuclein</term><term>proteasome</term><term>protein accumulation</term><term>ubiquitin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proteasome Endopeptidase Complex</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Central Nervous System</term><term>Parkinson Disease</term><term>Proteasome Endopeptidase Complex</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Age Factors</term><term>Animals</term><term>Humans</term><term>Models, Biological</term><term>Mutation</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Multicatalytic endopeptidase complex</term><term>Parkinson maladie</term><term>Protéine</term><term>Système nerveux pathologie</term><term>Ubiquitine</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 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="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name></region><name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. 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