Latrotoxin-like properties of a protein from brain

In bovine brain cortex cytoplasm we have identified a soluble protein (L-protein) of M r ∼90 kDa interacting with polyclonal antibodies to α-latrotoxin. The L-protein forms potential-dependent and cation-selective ion channels in BLM, which are blocked by Cd 2+. The fusogenic activity of the L-prote...

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Bibliographic Details
Published in:FEBS letters 1992-04, Vol.300 (3), p.219-221
Main Authors: Zhukareva, V.A., Shatursky, O.Ya, Lishko, V.K., Malysheva, M.K., Terletskaya, Ya.T., Tsygankova, O.M., Grishin, E.V.
Format: Article
Language:English
Subjects:
Animals
Bilayer lipid membrane
Biochemistry and metabolism
Biological and medical sciences
BLM
Bovine brain
Cattle
Central nervous system
Cerebral Cortex - chemistry
Channel
dipicolinie acid
DPA
Fundamental and applied biological sciences. Psychology
L-protein
Latrotoxin
Lipid Bilayers - chemistry
Liposome fusion
Liposomes - chemistry
Membrane Potentials
Molecular Weight
Nerve Tissue Proteins - chemistry
Nerve Tissue Proteins - isolation & purification
phosphatidylcholine
phosphatidylcthanolamine
SDS
sodium dodecyl sulfate
Solubility
Spider Venoms - chemistry
Tris
tris(hydroxymethyl)aminomethine
Vertebrates: nervous system and sense organs
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Summary:In bovine brain cortex cytoplasm we have identified a soluble protein (L-protein) of M r ∼90 kDa interacting with polyclonal antibodies to α-latrotoxin. The L-protein forms potential-dependent and cation-selective ion channels in BLM, which are blocked by Cd 2+. The fusogenic activity of the L-protein was demonstrated on liposomes. We have arrived at the conclusion that the action mechanisms of the L-protein and α-latrotoxin are similar.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)80849-C