Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson's disease
Identifieur interne : 001719 ( Main/Exploration ); précédent : 001718; suivant : 001720Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson's disease
Auteurs : Kevin St. P. Mcnaught [États-Unis] ; C. Warren Olanow [États-Unis]Source :
- Annals of Neurology [ 0364-5134 ] ; 2003.
Abstract
The etiopathogenesis of Parkinson's disease (PD) has been elusive. Recently, several lines of evidence have converged to suggest that defects in the ubiquitin‐proteasome system and proteolytic stress underlie nigral pathology in both familial and sporadic forms of the illness. In support of this concept, mutations in α‐synuclein that cause the protein to misfold and resist proteasomal degradation cause familial PD. Similarly, mutations in two enzymes involved in the normal function of the ubiquitin‐proteasome system, parkin and ubiquitin C‐terminal hydrolase L1, are also associated with hereditary PD. Furthermore, structural and function defects in 26/20S proteasomes with accumulation and aggregation of potentially cytotoxic abnormal proteins have been identified in the substantia nigra pars compacta of patients with sporadic PD. Thus, a defect in protein handling appears to be a common factor in sporadic and the various familial forms of PD. This hypothesis may also account for the vulnerability of the substantia nigra pars compacta in PD, why the disorder is age related, and the nature of the Lewy body. It has also facilitated the development of experimental models that recapitulate the behavioral and pathological features of PD, and hopefully will lead to the development of novel neuroprotective therapies for the disorder. Ann Neurol 2003;53 (suppl 3):S73–S86
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DOI: 10.1002/ana.10512
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Warren Olanow</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Department of Neurology, Mount Sinai School of Medicine, New York</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Annals of Neurology</title><title level="j" type="sub">Official Journal of the American Neurological Association and the Child Neurology Society</title><title level="j" type="abbrev">Ann Neurol.</title><idno type="ISSN">0364-5134</idno><idno type="eISSN">1531-8249</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2003">2003</date><biblScope unit="volume">53</biblScope><biblScope unit="issue">S3</biblScope><biblScope unit="supplement">3</biblScope><biblScope unit="page" from="S73">S73</biblScope><biblScope unit="page" to="S86">S86</biblScope></imprint><idno type="ISSN">0364-5134</idno></series><idno type="istex">3C4391AA6CDA5EAA41A260523BB2749A7067E48E</idno><idno type="DOI">10.1002/ana.10512</idno><idno type="ArticleID">ANA10512</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0364-5134</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The etiopathogenesis of Parkinson's disease (PD) has been elusive. Recently, several lines of evidence have converged to suggest that defects in the ubiquitin‐proteasome system and proteolytic stress underlie nigral pathology in both familial and sporadic forms of the illness. In support of this concept, mutations in α‐synuclein that cause the protein to misfold and resist proteasomal degradation cause familial PD. Similarly, mutations in two enzymes involved in the normal function of the ubiquitin‐proteasome system, parkin and ubiquitin C‐terminal hydrolase L1, are also associated with hereditary PD. Furthermore, structural and function defects in 26/20S proteasomes with accumulation and aggregation of potentially cytotoxic abnormal proteins have been identified in the substantia nigra pars compacta of patients with sporadic PD. Thus, a defect in protein handling appears to be a common factor in sporadic and the various familial forms of PD. This hypothesis may also account for the vulnerability of the substantia nigra pars compacta in PD, why the disorder is age related, and the nature of the Lewy body. It has also facilitated the development of experimental models that recapitulate the behavioral and pathological features of PD, and hopefully will lead to the development of novel neuroprotective therapies for the disorder. Ann Neurol 2003;53 (suppl 3):S73–S86</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="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. Mcnaught</name></region><name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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