Clues to How Alpha-Synuclein Damages Neurons in Parkinson's Disease
Identifieur interne : 002736 ( Main/Merge ); précédent : 002735; suivant : 002737Clues to How Alpha-Synuclein Damages Neurons in Parkinson's Disease
Auteurs : David Sulzer [États-Unis]Source :
- Movement disorders [ 0885-3185 ] ; 2010.
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Abstract
Alpha-synuclein (α-syn) appears to normally regulate neurotransmitter release, possibly via calcium-dependent binding and dissociation from lipid domains on secretory vesicles. The pathogenic effects of α-syn leading to Parkinson's disease (PD) appear to result from alternate toxic effects on lipid membrane. A variety of findings indicate that overexpression of wild-type α-syn, pathogenic mutations of α-syn, and dopamine-modified-α-syn promote toxic interaction between α-syn oligomers and lipids. These may disrupt transmembrane concentration gradients across secretory vesicles and other organelles and interfere with normal lysosomal or ubiqutin/proteasome mediated protein degradation or mitochondrial function. Additional causes of PD may interfere at other points with normal handling and degradation of α-syn, providing a variety of entry points to a converging neurodegenerative path underlying the disease.
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en" level="a">Clues to How Alpha-Synuclein Damages Neurons in Parkinson's Disease</title><author><name sortKey="Sulzer, David" sort="Sulzer, David" uniqKey="Sulzer D" first="David" last="Sulzer">David Sulzer</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>Departments of Neurology, Pharmacology, and Psychiatry, Columbia University Medical School; New York State Psychiatric Institute</s1><s2>New York, New York</s2><s3>USA</s3><sZ>1 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">État de New York</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">10-0193439</idno><date when="2010">2010</date><idno type="stanalyst">PASCAL 10-0193439 INIST</idno><idno type="RBID">Pascal:10-0193439</idno><idno type="wicri:Area/PascalFrancis/Corpus">000B97</idno><idno type="wicri:Area/PascalFrancis/Curation">002122</idno><idno type="wicri:Area/PascalFrancis/Checkpoint">000B49</idno><idno type="wicri:doubleKey">0885-3185:2010:Sulzer D:clues:to:how</idno><idno type="wicri:Area/Main/Merge">002736</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Clues to How Alpha-Synuclein Damages Neurons in Parkinson's Disease</title><author><name sortKey="Sulzer, David" sort="Sulzer, David" uniqKey="Sulzer D" first="David" last="Sulzer">David Sulzer</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>Departments of Neurology, Pharmacology, and Psychiatry, Columbia University Medical School; New York State Psychiatric Institute</s1><s2>New York, New York</s2><s3>USA</s3><sZ>1 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">État de New York</region></placeName></affiliation></author></analytic><series><title level="j" type="main">Movement disorders</title><title level="j" type="abbreviated">Mov. disord.</title><idno type="ISSN">0885-3185</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Movement disorders</title><title level="j" type="abbreviated">Mov. disord.</title><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Nervous system diseases</term><term>Neuron</term><term>Parkinson disease</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Maladie de Parkinson</term><term>Pathologie du système nerveux</term><term>Neurone</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alpha-synuclein (α-syn) appears to normally regulate neurotransmitter release, possibly via calcium-dependent binding and dissociation from lipid domains on secretory vesicles. The pathogenic effects of α-syn leading to Parkinson's disease (PD) appear to result from alternate toxic effects on lipid membrane. A variety of findings indicate that overexpression of wild-type α-syn, pathogenic mutations of α-syn, and dopamine-modified-α-syn promote toxic interaction between α-syn oligomers and lipids. These may disrupt transmembrane concentration gradients across secretory vesicles and other organelles and interfere with normal lysosomal or ubiqutin/proteasome mediated protein degradation or mitochondrial function. Additional causes of PD may interfere at other points with normal handling and degradation of α-syn, providing a variety of entry points to a converging neurodegenerative path underlying the disease.</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="Sulzer, David" sort="Sulzer, David" uniqKey="Sulzer D" first="David" last="Sulzer">David Sulzer</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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