Journal of Biological Chemistry · 1992 · 410 citations · 33 references
Life SciencesMolecular BiologyPhysiologyElectrophysiologyMolecular PhysiologyNeurophysiologyCalcium SignalingCardiac Ion ChannelsIntracellular Calcium SignalingIon Channel ExpressionIon Channel PhysiologyIon ChannelsCalcium Channel FunctionCalcium Channel PhysiologyCalcium Ion SignalingCurrent-voltage RelationsCurrent-voltage RelationshipCurrentsL-type Calcium CurrentVoltage-gated Calcium Channels
The skeletal muscle dihydropyridine receptor/Ca2+ channel is composed of five protein components (alpha 1, alpha 2 delta, beta, and gamma). Only two such components, alpha 1 and alpha 2, have been identified in heart. The present study reports the cloning and expression of a novel beta gene that is expressed in heart, lung, and brain. Coexpression of this beta with a cardiac alpha 1 in Xenopus oocytes causes the following changes in Ca2+ channel activity: it increases peak currents, accelerates activation kinetics, and shifts the current-voltage relationship toward more hyperpolarized potentials. It also increases dihydropyridine binding to alpha 1 in COS cells. These results indicate that the cardiac L-type Ca2+ channel has a similar subunit structure as in skeletal muscle, and provides evidence for the modulatory role of the beta subunit.
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Primary structure of the receptor for calcium channel blockers from skeletal muscle
Tsutomu Tanabe, Hiroshi Takeshima, Atsushi Mikami et al. · Nature · 1987 · 1.4K citations