Ubiquitin-proteasome system and Parkinson's disease.
Identifieur interne : 001841 ( Ncbi/Curation ); précédent : 001840; suivant : 001842Ubiquitin-proteasome system and Parkinson's disease.
Auteurs : C Warren Olanow [États-Unis] ; Kevin St P. McnaughtSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2006.
English descriptors
- KwdEn :
- 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.
DOI: 10.1002/mds.21013
PubMed: 16972273
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pubmed:16972273Le document en format XML
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<author><name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C Warren" last="Olanow">C Warren Olanow</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York10029, USA. warren.olanow@mssm.edu</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Neurology, Mount Sinai School of Medicine, New York, New York10029</wicri:regionArea>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Ubiquitin-proteasome system and Parkinson's disease.</title>
<author><name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C Warren" last="Olanow">C Warren Olanow</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York10029, USA. warren.olanow@mssm.edu</nlm:affiliation>
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<author><name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St P" last="Mcnaught">Kevin St P. Mcnaught</name>
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<series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title>
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<term>Animals</term>
<term>Central Nervous System (metabolism)</term>
<term>Humans</term>
<term>Models, Biological</term>
<term>Mutation</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Proteasome Endopeptidase Complex (genetics)</term>
<term>Proteasome Endopeptidase Complex (metabolism)</term>
<term>Ubiquitin (genetics)</term>
<term>Ubiquitin (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proteasome Endopeptidase Complex</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term>
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<term>Proteasome Endopeptidase Complex</term>
<term>Ubiquitin</term>
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<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.</div>
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