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• W2043759997 abstract "Cardiac L-type Ca2+ channels are multisubunit complexes composed of α1C, α2δ, and β2 subunits. We tested the roles of these subunits in forming a functional complex by characterizing the effects of subunit composition on dihydropyridine binding, its allosteric regulation, and the ability of dihydropyridines to inhibit channel activity. Transfection of COS.M6 cells with cardiac α1C-a (α1) led to the appearance of dihydropyridine ([3H]PN200-110) binding which was increased by coexpression of cardiac β2a (β), α2δa (α2), and the skeletal muscle γ. Maximum binding was achieved when cells expressed α1, β, and α2. Cells transfected with α1 and β had a binding affinity that was 5-10-fold lower than that observed in cardiac membranes. Coexpression of α2 normalized this affinity.(-)-D600 and diltiazem both partially inhibited PN200-110 binding to cardiac microsomes, but stimulated binding in cells transfected with α1 and β. Again, coexpression of α2 normalized this allosteric regulation. Therefore coexpression of α1β and α2 completely reconstituted high affinity dihydropyridine binding and its allosteric regulation as observed in cardiac membranes. Skeletal muscle γ was not required for this reconstitution. Expression in Xenopus oocytes demonstrated that coexpression of α2 with α1β increased the potency and maximum extent of block of Ca2+ channel currents by nisoldipine, a dihydropyridine Ca2+ channel antagonist. Our results demonstrate that α2 subunits are essential components of the cardiac L-type Ca2+ channel and predict a minimum subunit composition of α1Cβ2α2δ for this channel. Cardiac L-type Ca2+ channels are multisubunit complexes composed of α1C, α2δ, and β2 subunits. We tested the roles of these subunits in forming a functional complex by characterizing the effects of subunit composition on dihydropyridine binding, its allosteric regulation, and the ability of dihydropyridines to inhibit channel activity. Transfection of COS.M6 cells with cardiac α1C-a (α1) led to the appearance of dihydropyridine ([3H]PN200-110) binding which was increased by coexpression of cardiac β2a (β), α2δa (α2), and the skeletal muscle γ. Maximum binding was achieved when cells expressed α1, β, and α2. Cells transfected with α1 and β had a binding affinity that was 5-10-fold lower than that observed in cardiac membranes. Coexpression of α2 normalized this affinity.(-)-D600 and diltiazem both partially inhibited PN200-110 binding to cardiac microsomes, but stimulated binding in cells transfected with α1 and β. Again, coexpression of α2 normalized this allosteric regulation. Therefore coexpression of α1β and α2 completely reconstituted high affinity dihydropyridine binding and its allosteric regulation as observed in cardiac membranes. Skeletal muscle γ was not required for this reconstitution. Expression in Xenopus oocytes demonstrated that coexpression of α2 with α1β increased the potency and maximum extent of block of Ca2+ channel currents by nisoldipine, a dihydropyridine Ca2+ channel antagonist. Our results demonstrate that α2 subunits are essential components of the cardiac L-type Ca2+ channel and predict a minimum subunit composition of α1Cβ2α2δ for this channel." @default.
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• W2043759997 date "1995-11-01" @default.
• W2043759997 modified "2023-10-07" @default.
• W2043759997 title "Molecular Determinants of Cardiac Ca2+ Channel Pharmacology" @default.
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• W2043759997 doi "https://doi.org/10.1074/jbc.270.45.27106" @default.
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