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Characterization of the omega-conotoxin-binding molecule in rat brain synaptosomes and cultured neurons

B Marqueze, N Martin-Moutot, C Leveque and F Couraud

Laboratoire de Biochimie, CNRS UA 1179, Faculte de Medecine Nord, Marseille, France.

omega-Conotoxin GVIA is a peptide purified from the venom of the marine snail, Conus geographus, that specifically blocks voltage-sensitive calcium channels in neurons. A mono-[125I]iodo-omega-conotoxin was prepared and specific binding to both rat brain synaptosomal membranes and cultured neurons was detected. The interaction was irreversible and the association kinetic constant k was measured at 5-7 X 10(6) M-1 s-1 in synaptosomes and at 2-4 X 10(6) M-1 s-1 on intact neurons. The binding site capacities were 650 and 60 fmol/mg of protein, respectively. No competition was detected with other calcium channel blockers or with toxins acting on Na+ or K+ channels but the binding was lowered by the divalent cations Co2+ and Ca2+. Photoaffinity experiments specifically labeled a single component with an apparent Mr of 222,000 +/- 7,000 in brain synaptosomes and 245,000-300,000 in cultured embryonic neurons.

Volume 34, Issue 2, pp. 87-90, 08/01/1988
Copyright © 1988 by American Society for Pharmacology and Experimental Therapeutics




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Copyright © 1988 by the American Society for Pharmacology and Experimental Therapeutics