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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
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pubmed:dateCreated |
1996-11-19
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pubmed:databankReference | |
pubmed:abstractText |
alpha-Latrotoxin, a black widow spider neurotoxin, can bind to high affinity receptors on the presynaptic plasma membrane and stimulate massive neurotransmitter release in the absence of Ca2+. Neurexins, previously isolated as alpha-latrotoxin receptors, require Ca2+ for their interaction with the toxin and, thus, may not participate in the Ca2+-independent alpha-latrotoxin activity. We now report the isolation of a novel protein that binds alpha-latrotoxin with high affinity in the presence of various divalent cations (Ca2+, Mg2+, Ba2+, and Sr2+) as well as in EDTA. This protein, termed here latrophilin, has been purified from detergent-solubilized bovine brain membranes by affinity chromatography on immobilized alpha-latrotoxin and concentrated on a wheat germ agglutinin affinity column. The single polypeptide chain of latrophilin is N-glycosylated and has an apparent molecular weight of 120,000. Sucrose gradient centrifugations demonstrated that latrophilin and alpha-latrotoxin form a stable equimolar complex. In the presence of the toxin, anti-alpha-latrotoxin antibodies precipitated iodinated latrophilin, whose binding to immobilized toxin was characterized by a dissociation constant of 0.5-0.7 nM. This presumably membrane-bound protein is localized to and differentially distributed among neuronal tissues, with about four times more latrophilin expressed in the cerebral cortex than in the cerebellum; subcellular fractionation showed that the protein is highly enriched in synaptosomal plasma membranes. Our data suggest that latrophilin may represent the Ca2+-independent receptor and/or molecular target for alpha-latrotoxin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Spider Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-latrotoxin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-latrotoxin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23239-45
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:8798521-Amino Acid Sequence,
pubmed-meshheading:8798521-Animals,
pubmed-meshheading:8798521-Calcium,
pubmed-meshheading:8798521-Cattle,
pubmed-meshheading:8798521-Membrane Glycoproteins,
pubmed-meshheading:8798521-Molecular Sequence Data,
pubmed-meshheading:8798521-Nerve Tissue Proteins,
pubmed-meshheading:8798521-Protein Binding,
pubmed-meshheading:8798521-Rats,
pubmed-meshheading:8798521-Receptors, Peptide,
pubmed-meshheading:8798521-Sequence Analysis,
pubmed-meshheading:8798521-Species Specificity,
pubmed-meshheading:8798521-Spider Venoms,
pubmed-meshheading:8798521-Synaptosomes,
pubmed-meshheading:8798521-Tissue Distribution
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pubmed:year |
1996
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pubmed:articleTitle |
Isolation and biochemical characterization of a Ca2+-independent alpha-latrotoxin-binding protein.
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pubmed:affiliation |
Department of Biochemistry, Imperial College, London, SW7 2AY, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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