Alpha-synuclein and Parkinson's disease.
Identifieur interne : 000173 ( Ncbi/Curation ); précédent : 000172; suivant : 000174Alpha-synuclein and Parkinson's disease.
Auteurs : C B Lücking [France] ; A. BriceSource :
- Cellular and molecular life sciences : CMLS [ 1420-682X ] ; 2000.
English descriptors
- KwdEn :
- 14-3-3 Proteins, Alzheimer Disease (metabolism), Alzheimer Disease (pathology), Amyotrophic Lateral Sclerosis (metabolism), Amyotrophic Lateral Sclerosis (pathology), Animals, Carrier Proteins (metabolism), Cell Differentiation, Cell Survival, Dopamine (metabolism), Humans, Molecular Chaperones (metabolism), Multiple System Atrophy (metabolism), Multiple System Atrophy (pathology), Nerve Tissue Proteins (chemistry), Nerve Tissue Proteins (genetics), Nerve Tissue Proteins (metabolism), Nerve Tissue Proteins (toxicity), Neuronal Plasticity, Neurons (cytology), Neurons (metabolism), Neurons (pathology), Parkinson Disease (genetics), Parkinson Disease (metabolism), Parkinson Disease (pathology), Protein Structure, Tertiary, Synucleins, Tyrosine 3-Monooxygenase (metabolism), alpha-Synuclein, tau Proteins (metabolism).
- MESH :
- chemical , chemistry : Nerve Tissue Proteins.
- chemical , genetics : Nerve Tissue Proteins.
- chemical , metabolism : Carrier Proteins, Dopamine, Molecular Chaperones, Nerve Tissue Proteins, Tyrosine 3-Monooxygenase, tau Proteins.
- chemical , toxicity : Nerve Tissue Proteins.
- chemical : 14-3-3 Proteins, Synucleins, alpha-Synuclein.
- cytology : Neurons.
- genetics : Parkinson Disease.
- metabolism : Alzheimer Disease, Amyotrophic Lateral Sclerosis, Multiple System Atrophy, Neurons, Parkinson Disease.
- pathology : Alzheimer Disease, Amyotrophic Lateral Sclerosis, Multiple System Atrophy, Neurons, Parkinson Disease.
- Animals, Cell Differentiation, Cell Survival, Humans, Neuronal Plasticity, Protein Structure, Tertiary.
Abstract
The involvement of alpha-synuclein in neurodegenerative diseases was first suspected after the isolation of an alpha-synuclein fragment (NAC) from amyloid plaques in Alzheimer's disease (AD). Later, two different alpha-synuclein mutations were shown to be associated with autosomal-dominant Parkinson's disease (PD), but only in a small number of families. However, the discovery that alpha-synuclein is a major component of Lewy bodies and Lewy neurites, the pathological hallmarks of PD, confirmed its role in PD pathogenesis. Pathological aggregation of the protein might be responsible for neurodegeneration. In addition, soluble oligomers of alpha-synuclein might be even more toxic than the insoluble fibrils found in Lewy bodies. Multiple factors have been shown to accelerate alpha-synuclein aggregation in vitro. Therapeutic strategies aimed to prevent this aggregation are therefore envisaged. Although little has been learned about its normal function, alpha-synuclein appears to interact with a variety of proteins and membrane phospholipids, and may therefore participate in a number of signaling pathways. In particular, it may play a role in regulating cell differentiation, synaptic plasticity, cell survival, and dopaminergic neurotransmission. Thus, pathological mechanisms based on disrupted normal function are also possible.
DOI: 10.1007/PL00000671
PubMed: 11215516
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001281
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :001240
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :001240
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :000173
Links to Exploration step
pubmed:11215516Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Alpha-synuclein and Parkinson's disease.</title>
<author><name sortKey="Lucking, C B" sort="Lucking, C B" uniqKey="Lucking C" first="C B" last="Lücking">C B Lücking</name>
<affiliation wicri:level="3"><nlm:affiliation>H pital de la Salpetrière, INSERM U 289, Paris, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>H pital de la Salpetrière, INSERM U 289, Paris</wicri:regionArea>
<placeName><region type="region">Île-de-France</region>
<region type="old region">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Brice, A" sort="Brice, A" uniqKey="Brice A" first="A" last="Brice">A. Brice</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2000">2000</date>
<idno type="RBID">pubmed:11215516</idno>
<idno type="pmid">11215516</idno>
<idno type="doi">10.1007/PL00000671</idno>
<idno type="wicri:Area/PubMed/Corpus">001281</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001281</idno>
<idno type="wicri:Area/PubMed/Curation">001240</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001240</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001240</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001240</idno>
<idno type="wicri:Area/Ncbi/Merge">000173</idno>
<idno type="wicri:Area/Ncbi/Curation">000173</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Alpha-synuclein and Parkinson's disease.</title>
<author><name sortKey="Lucking, C B" sort="Lucking, C B" uniqKey="Lucking C" first="C B" last="Lücking">C B Lücking</name>
<affiliation wicri:level="3"><nlm:affiliation>H pital de la Salpetrière, INSERM U 289, Paris, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>H pital de la Salpetrière, INSERM U 289, Paris</wicri:regionArea>
<placeName><region type="region">Île-de-France</region>
<region type="old region">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Brice, A" sort="Brice, A" uniqKey="Brice A" first="A" last="Brice">A. Brice</name>
</author>
</analytic>
<series><title level="j">Cellular and molecular life sciences : CMLS</title>
<idno type="ISSN">1420-682X</idno>
<imprint><date when="2000" type="published">2000</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>14-3-3 Proteins</term>
<term>Alzheimer Disease (metabolism)</term>
<term>Alzheimer Disease (pathology)</term>
<term>Amyotrophic Lateral Sclerosis (metabolism)</term>
<term>Amyotrophic Lateral Sclerosis (pathology)</term>
<term>Animals</term>
<term>Carrier Proteins (metabolism)</term>
<term>Cell Differentiation</term>
<term>Cell Survival</term>
<term>Dopamine (metabolism)</term>
<term>Humans</term>
<term>Molecular Chaperones (metabolism)</term>
<term>Multiple System Atrophy (metabolism)</term>
<term>Multiple System Atrophy (pathology)</term>
<term>Nerve Tissue Proteins (chemistry)</term>
<term>Nerve Tissue Proteins (genetics)</term>
<term>Nerve Tissue Proteins (metabolism)</term>
<term>Nerve Tissue Proteins (toxicity)</term>
<term>Neuronal Plasticity</term>
<term>Neurons (cytology)</term>
<term>Neurons (metabolism)</term>
<term>Neurons (pathology)</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Parkinson Disease (pathology)</term>
<term>Protein Structure, Tertiary</term>
<term>Synucleins</term>
<term>Tyrosine 3-Monooxygenase (metabolism)</term>
<term>alpha-Synuclein</term>
<term>tau Proteins (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nerve Tissue Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nerve Tissue Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term>
<term>Dopamine</term>
<term>Molecular Chaperones</term>
<term>Nerve Tissue Proteins</term>
<term>Tyrosine 3-Monooxygenase</term>
<term>tau Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Nerve Tissue Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>14-3-3 Proteins</term>
<term>Synucleins</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Neurons</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term>
<term>Amyotrophic Lateral Sclerosis</term>
<term>Multiple System Atrophy</term>
<term>Neurons</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Alzheimer Disease</term>
<term>Amyotrophic Lateral Sclerosis</term>
<term>Multiple System Atrophy</term>
<term>Neurons</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Differentiation</term>
<term>Cell Survival</term>
<term>Humans</term>
<term>Neuronal Plasticity</term>
<term>Protein Structure, Tertiary</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The involvement of alpha-synuclein in neurodegenerative diseases was first suspected after the isolation of an alpha-synuclein fragment (NAC) from amyloid plaques in Alzheimer's disease (AD). Later, two different alpha-synuclein mutations were shown to be associated with autosomal-dominant Parkinson's disease (PD), but only in a small number of families. However, the discovery that alpha-synuclein is a major component of Lewy bodies and Lewy neurites, the pathological hallmarks of PD, confirmed its role in PD pathogenesis. Pathological aggregation of the protein might be responsible for neurodegeneration. In addition, soluble oligomers of alpha-synuclein might be even more toxic than the insoluble fibrils found in Lewy bodies. Multiple factors have been shown to accelerate alpha-synuclein aggregation in vitro. Therapeutic strategies aimed to prevent this aggregation are therefore envisaged. Although little has been learned about its normal function, alpha-synuclein appears to interact with a variety of proteins and membrane phospholipids, and may therefore participate in a number of signaling pathways. In particular, it may play a role in regulating cell differentiation, synaptic plasticity, cell survival, and dopaminergic neurotransmission. Thus, pathological mechanisms based on disrupted normal function are also possible.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Ncbi/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000173 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd -nk 000173 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= Ncbi |étape= Curation |type= RBID |clé= pubmed:11215516 |texte= Alpha-synuclein and Parkinson's disease. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/RBID.i -Sk "pubmed:11215516" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
This area was generated with Dilib version V0.6.29. |