Alpha-synuclein dysfunction in Lewy body diseases.
Identifieur interne : 002F38 ( PubMed/Corpus ); précédent : 002F37; suivant : 002F39Alpha-synuclein dysfunction in Lewy body diseases.
Auteurs : George K. Tofaris ; Maria Grazia SpillantiniSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2005.
English descriptors
- KwdEn :
- Animals, Chromosomes, Human, Pair 6 (genetics), Cytoskeleton (metabolism), Drosophila, Humans, In Vitro Techniques, Lewy Body Disease (genetics), Lewy Body Disease (metabolism), Lewy Body Disease (physiopathology), Mice, Parkinson Disease (genetics), Parkinson Disease (physiopathology), Phenotype, Phosphorylation, Point Mutation (genetics), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , genetics : alpha-Synuclein.
- genetics : Chromosomes, Human, Pair 6, Lewy Body Disease, Parkinson Disease, Point Mutation.
- metabolism : Cytoskeleton, Lewy Body Disease, alpha-Synuclein.
- physiopathology : Lewy Body Disease, Parkinson Disease.
- Animals, Drosophila, Humans, In Vitro Techniques, Mice, Phenotype, Phosphorylation.
Abstract
alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Its relevance to Parkinson's disease (PD) is based on mutations found in familial cases of the disease and its presence in filaments of Lewy bodies (LB) and Lewy neurites (LN) in sporadic cases where it is packed in a beta-sheet configuration. This structural plasticity of alpha-synuclein has raised the possibility that neurodegeneration may be a consequence of abnormal protein folding. The extent to which abnormal folding and aggregation of neuronal proteins is directly toxic to the cell, an inert biochemical marker of an underlying harmful metabolic defect, or a protective reaction remains to be seen. We review the function of alpha-synuclein and recent studies that have shed light on the mechanisms by which it aggregates.
DOI: 10.1002/mds.20538
PubMed: 16092089
Links to Exploration step
pubmed:16092089Le document en format XML
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<author><name sortKey="Spillantini, Maria Grazia" sort="Spillantini, Maria Grazia" uniqKey="Spillantini M" first="Maria Grazia" last="Spillantini">Maria Grazia Spillantini</name>
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<front><div type="abstract" xml:lang="en">alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Its relevance to Parkinson's disease (PD) is based on mutations found in familial cases of the disease and its presence in filaments of Lewy bodies (LB) and Lewy neurites (LN) in sporadic cases where it is packed in a beta-sheet configuration. This structural plasticity of alpha-synuclein has raised the possibility that neurodegeneration may be a consequence of abnormal protein folding. The extent to which abnormal folding and aggregation of neuronal proteins is directly toxic to the cell, an inert biochemical marker of an underlying harmful metabolic defect, or a protective reaction remains to be seen. We review the function of alpha-synuclein and recent studies that have shed light on the mechanisms by which it aggregates.</div>
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<CopyrightInformation>Copyright 2005 Movement Disorder Society.</CopyrightInformation>
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