Inhibition of beta-bungarotoxin binding to brain membranes by mast cell degranulating peptide, toxin I, and ethylene glycol bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid.
The presynaptically active snake venom neurotoxin beta-bungarotoxin (beta-Butx) is known to affect neurotransmitter release by binding to a subtype of voltage-activated K+ channels. Here we show that mast cell degranulating (MCD) peptide from bee venom inhibits the binding of 125I-labeled beta-Butx to chick and rat brain membranes with apparent Ki values of 180 nM and 1100 nM, respectively. The mechanism of inhibition by MCD peptide is noncompetitive, as is inhibition of 125I-beta-Butx binding by the protease inhibitor homologue from mamba venom, toxin I. Beta-Butx and its binding antagonists thus bind to different sites of the same membrane protein. Removal of Ca2+ by ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid inhibits the binding of 125I-beta-Butx by lowering its affinity to brain membranes.
D000818:Animals; D001514:Bee Venoms / Q000494:pharmacology*; D001921:Brain / Q000378:metabolism*; D002038:Bungarotoxins / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D004533:Egtazic Acid / Q000494:pharmacology*; D004546:Elapid Venoms / Q000494:pharmacology*; D007700:Kinetics; D010455:Peptides / Q000494:pharmacology*; D051381:Rats; D013329:Structure-Activity Relationship
D001514:Bee Venoms; D002038:Bungarotoxins; D002352:Carrier Proteins; D004546:Elapid Venoms; D010455:Peptides; C041451:beta-bungarotoxin binding protein, rat; C034915:toxin I, black mamba venom; C008331:mast cell degranulating peptide; D004533:Egtazic Acid; D002118:Calcium