Brain proteasomal function in sporadic Parkinson's disease and related disorders.
Identifieur interne : 000239 ( Ncbi/Checkpoint ); précédent : 000238; suivant : 000240Brain proteasomal function in sporadic Parkinson's disease and related disorders.
Auteurs : Yoshiaki Furukawa [Canada] ; Sophie Vigouroux ; Henry Wong ; Mark Guttman ; Ali H. Rajput ; Lee Ang ; Marièle Briand ; Stephen J. Kish ; Yves BriandSource :
- Annals of neurology [ 0364-5134 ] ; 2002.
English descriptors
- KwdEn :
- Aged, Brain (enzymology), Brain (physiology), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Humans, Multienzyme Complexes (genetics), Multienzyme Complexes (metabolism), Multiple System Atrophy (enzymology), Multiple System Atrophy (genetics), Parkinson Disease (enzymology), Parkinson Disease (genetics), Peptide Hydrolases (metabolism), Proteasome Endopeptidase Complex, Supranuclear Palsy, Progressive (enzymology), Supranuclear Palsy, Progressive (genetics).
- MESH :
- chemical , genetics : Cysteine Endopeptidases, Multienzyme Complexes.
- enzymology : Brain, Multiple System Atrophy, Parkinson Disease, Supranuclear Palsy, Progressive.
- genetics : Multiple System Atrophy, Parkinson Disease, Supranuclear Palsy, Progressive.
- chemical , metabolism : Cysteine Endopeptidases, Multienzyme Complexes, Peptide Hydrolases.
- physiology : Brain.
- Aged, Humans, Proteasome Endopeptidase Complex.
Abstract
Because genetic defects relating to the ubiquitin-proteasome system were reported in familial parkinsonism, we evaluated proteasomal function in autopsied brains with sporadic Parkinson's disease. We found that proteasome peptidase activities in a fraction specific to the proteasome were preserved in five brain areas (including the striatum) of Parkinson's disease where neuronal loss is not observed. Striatal protein levels of two proteasome subunits were normal in Parkinson's disease but reduced mildly in disease controls (multiple system atrophy). Our brain data suggest that a systemic, global disturbance in the catalytic activity and degradation ability of the proteasome itself is unlikely to explain the cause of Parkinson's disease.
DOI: 10.1002/ana.10207
PubMed: 12112087
Affiliations:
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Rajput</name></author><author><name sortKey="Ang, Lee" sort="Ang, Lee" uniqKey="Ang L" first="Lee" last="Ang">Lee Ang</name></author><author><name sortKey="Briand, Mariele" sort="Briand, Mariele" uniqKey="Briand M" first="Marièle" last="Briand">Marièle Briand</name></author><author><name sortKey="Kish, Stephen J" sort="Kish, Stephen J" uniqKey="Kish S" first="Stephen J" last="Kish">Stephen J. 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Rajput</name></author><author><name sortKey="Ang, Lee" sort="Ang, Lee" uniqKey="Ang L" first="Lee" last="Ang">Lee Ang</name></author><author><name sortKey="Briand, Mariele" sort="Briand, Mariele" uniqKey="Briand M" first="Marièle" last="Briand">Marièle Briand</name></author><author><name sortKey="Kish, Stephen J" sort="Kish, Stephen J" uniqKey="Kish S" first="Stephen J" last="Kish">Stephen J. Kish</name></author><author><name sortKey="Briand, Yves" sort="Briand, Yves" uniqKey="Briand Y" first="Yves" last="Briand">Yves Briand</name></author></analytic><series><title level="j">Annals of neurology</title><idno type="ISSN">0364-5134</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aged</term><term>Brain (enzymology)</term><term>Brain (physiology)</term><term>Cysteine Endopeptidases (genetics)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Humans</term><term>Multienzyme Complexes (genetics)</term><term>Multienzyme Complexes (metabolism)</term><term>Multiple System Atrophy (enzymology)</term><term>Multiple System Atrophy (genetics)</term><term>Parkinson Disease (enzymology)</term><term>Parkinson Disease (genetics)</term><term>Peptide Hydrolases (metabolism)</term><term>Proteasome Endopeptidase Complex</term><term>Supranuclear Palsy, Progressive (enzymology)</term><term>Supranuclear Palsy, Progressive (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Multienzyme Complexes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Brain</term><term>Multiple System Atrophy</term><term>Parkinson Disease</term><term>Supranuclear Palsy, Progressive</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Multiple System Atrophy</term><term>Parkinson Disease</term><term>Supranuclear Palsy, Progressive</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Multienzyme Complexes</term><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Aged</term><term>Humans</term><term>Proteasome Endopeptidase Complex</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Because genetic defects relating to the ubiquitin-proteasome system were reported in familial parkinsonism, we evaluated proteasomal function in autopsied brains with sporadic Parkinson's disease. We found that proteasome peptidase activities in a fraction specific to the proteasome were preserved in five brain areas (including the striatum) of Parkinson's disease where neuronal loss is not observed. Striatal protein levels of two proteasome subunits were normal in Parkinson's disease but reduced mildly in disease controls (multiple system atrophy). Our brain data suggest that a systemic, global disturbance in the catalytic activity and degradation ability of the proteasome itself is unlikely to explain the cause of Parkinson's disease.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Ang, Lee" sort="Ang, Lee" uniqKey="Ang L" first="Lee" last="Ang">Lee Ang</name><name sortKey="Briand, Mariele" sort="Briand, Mariele" uniqKey="Briand M" first="Marièle" last="Briand">Marièle Briand</name><name sortKey="Briand, Yves" sort="Briand, Yves" uniqKey="Briand Y" first="Yves" last="Briand">Yves Briand</name><name sortKey="Guttman, Mark" sort="Guttman, Mark" uniqKey="Guttman M" first="Mark" last="Guttman">Mark Guttman</name><name sortKey="Kish, Stephen J" sort="Kish, Stephen J" uniqKey="Kish S" first="Stephen J" last="Kish">Stephen J. Kish</name><name sortKey="Rajput, Ali H" sort="Rajput, Ali H" uniqKey="Rajput A" first="Ali H" last="Rajput">Ali H. Rajput</name><name sortKey="Vigouroux, Sophie" sort="Vigouroux, Sophie" uniqKey="Vigouroux S" first="Sophie" last="Vigouroux">Sophie Vigouroux</name><name sortKey="Wong, Henry" sort="Wong, Henry" uniqKey="Wong H" first="Henry" last="Wong">Henry Wong</name></noCountry><country name="Canada"><noRegion><name sortKey="Furukawa, Yoshiaki" sort="Furukawa, Yoshiaki" uniqKey="Furukawa Y" first="Yoshiaki" last="Furukawa">Yoshiaki Furukawa</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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