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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-10-30
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pubmed:abstractText |
We characterized beta-synuclein, the non-amyloidogenic homolog of alpha-synuclein, as an inhibitor of aggregation of alpha-synuclein, a molecule implicated in Parkinson's disease. For this, doubly transgenic mice expressing human (h) alpha- and beta-synuclein were generated. In doubly transgenic mice, beta-synuclein ameliorated motor deficits, neurodegenerative alterations, and neuronal alpha-synuclein accumulation seen in halpha-synuclein transgenic mice. Similarly, cell lines transfected with beta-synuclein were resistant to alpha-synuclein accumulation. halpha-synuclein was coimmunoprecipitated with hbeta-synuclein in the brains of doubly transgenic mice and in the double-transfected cell lines. Our results raise the possibility that beta-synuclein might be a natural negative regulator of alpha-synuclein aggregation and that a similar class of endogenous factors might regulate the aggregation state of other molecules involved in neurodegeneration. Such an anti-amyloidogenic property of beta-synuclein might also provide a novel strategy for the treatment of neurodegenerative disorders.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antiparkinson Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNCB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Snca protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sncb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Synuclein
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
213-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11683992-Animals,
pubmed-meshheading:11683992-Antiparkinson Agents,
pubmed-meshheading:11683992-Brain,
pubmed-meshheading:11683992-Dimerization,
pubmed-meshheading:11683992-Gene Expression,
pubmed-meshheading:11683992-Humans,
pubmed-meshheading:11683992-Immunosorbent Techniques,
pubmed-meshheading:11683992-Mice,
pubmed-meshheading:11683992-Mice, Inbred C57BL,
pubmed-meshheading:11683992-Mice, Inbred DBA,
pubmed-meshheading:11683992-Mice, Transgenic,
pubmed-meshheading:11683992-Motor Activity,
pubmed-meshheading:11683992-Nerve Tissue Proteins,
pubmed-meshheading:11683992-Neurodegenerative Diseases,
pubmed-meshheading:11683992-Recombinant Proteins,
pubmed-meshheading:11683992-Synucleins,
pubmed-meshheading:11683992-Transfection,
pubmed-meshheading:11683992-alpha-Synuclein,
pubmed-meshheading:11683992-beta-Synuclein
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pubmed:year |
2001
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pubmed:articleTitle |
beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor.
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pubmed:affiliation |
Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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