Mapacalcine is a small protein (Mr = 19041) composed of two homologous chains purified from the marine sponge Cliona vastifica. Recently, we demonstrated that it was able to specifically block a Ca2+ channel which could not be related to already described channels on mouse intestinal myocytes. This Ca2+ current was insensitive to the known peptidic and organic calcium channel blockers. Mapacalcine was ineffective on T-type and L-type Ca2+ currents present on rat portal vein myocytes [Morel, Drobecq, Sautière, Tartar, Mironneau, Qar, Lavie, and Hugues (1997) Mol. Pharmacol. 51, 1042–1052]. We report here the preparation and purification of a monoiodo-derivative of mapa-calcine which retains its biological properties. Binding parameters of mapacalcine to its receptors have been characterized on mouse intestinal membranes. It binds to its receptors with a Kd = 0.8 nM, and a maximal binding capacity of 171 fmol/mg of protein on membrane preparations. Our data show that we have prepared a tool that is usable for pharmacological studies of a receptor associated with a new type of calcium channel for which no ligand was available until now.

This content is only available as a PDF.