Recent advances on alpha-synuclein cell biology: functions and dysfunctions.
Identifieur interne : 003066 ( Main/Exploration ); précédent : 003065; suivant : 003067Recent advances on alpha-synuclein cell biology: functions and dysfunctions.
Auteurs : C. Alves Da Costa [France]Source :
- Current molecular medicine [ 1566-5240 ] ; 2003.
English descriptors
- KwdEn :
- Alzheimer Disease (etiology), Animals, Brain (physiology), Cell Death (physiology), Mice, Mice, Knockout, Nerve Tissue Proteins (genetics), Nerve Tissue Proteins (physiology), Neuronal Plasticity, Parkinson Disease (etiology), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Synapses (physiology), Synucleins, Transport Vesicles (physiology), alpha-Synuclein.
- MESH :
- chemical , genetics : Nerve Tissue Proteins, Recombinant Proteins.
- etiology : Alzheimer Disease, Parkinson Disease.
- chemical , metabolism : Recombinant Proteins.
- physiology : Brain, Cell Death, Nerve Tissue Proteins, Synapses, Transport Vesicles.
- Animals, Mice, Mice, Knockout, Neuronal Plasticity, Synucleins, alpha-Synuclein.
Abstract
Alpha-synuclein is a recently discovered protein that was first identified as the major non amyloid component of senile plaques, the cerebral lesion likely responsible for Alzheimer's disease. The role of alpha-synuclein in another brain disease namely Parkinson's disease, has been more deeply documented. It appears that alpha-synuclein fills up the intracytoplasmic inclusions called Lewy bodies that likely contribute to the etiology of Parkinson's disease. Furthermore, rare familial forms of Parkinson's disease have been shown to be linked to autosomal dominant mutations of alpha-synucleins. Is alpha-synuclein a bridge between Alzheimer's and Parkinson's diseases? Could it be seen as a common denominator for these two neurodegenerative diseases? These issues could be better addressed by further delineating the physiological function of alpha-synuclein and, as a corollary, the dysfunction taking place along with the diseases. Here, I will review the recent advances concerning the physiology of alpha-synuclein and will particularly focus on the post-traductional events leading to drastic biophysical transformations. I will describe recent works suggesting that these modifications directly modulate the normal function of alpha-synuclein, likely accounting for the dysfunction associated with Parkinson's disease and perhaps contributing to Alzheimer's pathology.
PubMed: 12558071
Affiliations:
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Alves Da Costa</name><affiliation wicri:level="3"><nlm:affiliation>IPMC du CNRS, UMR6097, 660 Route des Lucioles, Sophia Antipolis, 06560, Valbonne, France. acosta@ipmc.cnrs.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>IPMC du CNRS, UMR6097, 660 Route des Lucioles, Sophia Antipolis, 06560, Valbonne</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Valbonne</settlement></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003</date><idno type="RBID">pubmed:12558071</idno><idno type="pmid">12558071</idno><idno type="wicri:Area/PubMed/Corpus">001120</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001120</idno><idno type="wicri:Area/PubMed/Curation">001079</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001079</idno><idno type="wicri:Area/PubMed/Checkpoint">001079</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001079</idno><idno type="wicri:Area/Ncbi/Merge">000307</idno><idno type="wicri:Area/Ncbi/Curation">000307</idno><idno type="wicri:Area/Ncbi/Checkpoint">000307</idno><idno type="wicri:doubleKey">1566-5240:2003:Alves Da Costa C:recent:advances:on</idno><idno type="wicri:Area/Main/Merge">003509</idno><idno type="wicri:Area/Main/Curation">003066</idno><idno type="wicri:Area/Main/Exploration">003066</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Recent advances on alpha-synuclein cell biology: functions and dysfunctions.</title><author><name sortKey="Alves Da Costa, C" sort="Alves Da Costa, C" uniqKey="Alves Da Costa C" first="C" last="Alves Da Costa">C. Alves Da Costa</name><affiliation wicri:level="3"><nlm:affiliation>IPMC du CNRS, UMR6097, 660 Route des Lucioles, Sophia Antipolis, 06560, Valbonne, France. acosta@ipmc.cnrs.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>IPMC du CNRS, UMR6097, 660 Route des Lucioles, Sophia Antipolis, 06560, Valbonne</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Valbonne</settlement></placeName></affiliation></author></analytic><series><title level="j">Current molecular medicine</title><idno type="ISSN">1566-5240</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (etiology)</term><term>Animals</term><term>Brain (physiology)</term><term>Cell Death (physiology)</term><term>Mice</term><term>Mice, Knockout</term><term>Nerve Tissue Proteins (genetics)</term><term>Nerve Tissue Proteins (physiology)</term><term>Neuronal Plasticity</term><term>Parkinson Disease (etiology)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Synapses (physiology)</term><term>Synucleins</term><term>Transport Vesicles (physiology)</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nerve Tissue Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Brain</term><term>Cell Death</term><term>Nerve Tissue Proteins</term><term>Synapses</term><term>Transport Vesicles</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Mice, Knockout</term><term>Neuronal Plasticity</term><term>Synucleins</term><term>alpha-Synuclein</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alpha-synuclein is a recently discovered protein that was first identified as the major non amyloid component of senile plaques, the cerebral lesion likely responsible for Alzheimer's disease. The role of alpha-synuclein in another brain disease namely Parkinson's disease, has been more deeply documented. It appears that alpha-synuclein fills up the intracytoplasmic inclusions called Lewy bodies that likely contribute to the etiology of Parkinson's disease. Furthermore, rare familial forms of Parkinson's disease have been shown to be linked to autosomal dominant mutations of alpha-synucleins. Is alpha-synuclein a bridge between Alzheimer's and Parkinson's diseases? Could it be seen as a common denominator for these two neurodegenerative diseases? These issues could be better addressed by further delineating the physiological function of alpha-synuclein and, as a corollary, the dysfunction taking place along with the diseases. Here, I will review the recent advances concerning the physiology of alpha-synuclein and will particularly focus on the post-traductional events leading to drastic biophysical transformations. I will describe recent works suggesting that these modifications directly modulate the normal function of alpha-synuclein, likely accounting for the dysfunction associated with Parkinson's disease and perhaps contributing to Alzheimer's pathology.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Valbonne</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Alves Da Costa, C" sort="Alves Da Costa, C" uniqKey="Alves Da Costa C" first="C" last="Alves Da Costa">C. Alves Da Costa</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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