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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-12-17
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pubmed:abstractText |
Synaptophysin interacts with synaptobrevin in membranes of adult small synaptic vesicles. The synaptophysin/synaptobrevin complex promotes synaptobrevin to built up functional SNARE complexes thereby modulating synaptic efficiency. Synaptophysin in addition is a cholesterol-binding protein. Depleting the membranous cholesterol content by filipin or beta-methylcyclodextrin (beta-MCD) decreased the solubility of synaptophysin in Triton X-100 with less effects on synaptobrevin. In small synaptic vesicles from rat brain the synaptophysin/synaptobrevin complex was diminished upon beta-MCD treatment as revealed by chemical cross-linking. Mice with a genetic mutation in the Niemann-Pick C1 gene developing a defect in cholesterol sorting showed significantly reduced amounts of the synaptophysin/synaptobrevin complex compared to their homo- or heterozygous littermates. Finally when using primary cultures of mouse hippocampus the synaptophysin/synaptobrevin complex was down-regulated after depleting the endogenous cholesterol content by the HMG-CoA-reductase inhibitor lovastatin. Alternatively, treatment with cholesterol up-regulated the synaptophysin/synaptobrevin interaction in these cultures. These data indicate that the synaptophysin/synaptobrevin interaction critically depends on a high cholesterol content in the membrane of synaptic vesicles. Variations in the availability of cholesterol may promote or impair synaptic efficiency by interfering with this complex.
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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/Anticholesteremic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Filipin,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethylglutaryl-CoA...,
http://linkedlifedata.com/resource/pubmed/chemical/Lovastatin,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptophysin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-3042
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12485399-Animals,
pubmed-meshheading:12485399-Anticholesteremic Agents,
pubmed-meshheading:12485399-Brain,
pubmed-meshheading:12485399-CHO Cells,
pubmed-meshheading:12485399-Cholesterol,
pubmed-meshheading:12485399-Cricetinae,
pubmed-meshheading:12485399-Cyclodextrins,
pubmed-meshheading:12485399-Detergents,
pubmed-meshheading:12485399-Filipin,
pubmed-meshheading:12485399-Hydroxymethylglutaryl-CoA Reductase Inhibitors,
pubmed-meshheading:12485399-Lovastatin,
pubmed-meshheading:12485399-Membrane Proteins,
pubmed-meshheading:12485399-Membranes,
pubmed-meshheading:12485399-Mice,
pubmed-meshheading:12485399-Mice, Inbred BALB C,
pubmed-meshheading:12485399-Niemann-Pick Diseases,
pubmed-meshheading:12485399-Octoxynol,
pubmed-meshheading:12485399-Protein Transport,
pubmed-meshheading:12485399-R-SNARE Proteins,
pubmed-meshheading:12485399-Rats,
pubmed-meshheading:12485399-Solubility,
pubmed-meshheading:12485399-Synaptic Vesicles,
pubmed-meshheading:12485399-Synaptophysin,
pubmed-meshheading:12485399-Up-Regulation
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pubmed:year |
2003
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pubmed:articleTitle |
The synaptophysin/synaptobrevin interaction critically depends on the cholesterol content.
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pubmed:affiliation |
Institut für Anatomie der Charité, Mathematisch-natur-wissenschaftliche Fakultät I, Humboldt Universität zu Berlin, Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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