Voltage-gated L-type Ca2+ channels control depolarization-induced Ca2+ entr
y in different electrically excitable cells, including mammalian heart. Imp
ortant molecular and functional details providing new insight into L-type c
hannel structure and modulation are reviewed in this article. This includes
the identification of amino acid residues responsible for drug binding, th
e role of accessory subunits and alternative splicing for fine-tuning chann
el activity and modulation by protein kinases (A, C, tyrosine kinases), cGM
P-dependent pathways, calmodulin and Ca2+. Alterations in Ca2+ channel acti
vity under pathological conditions such as in heart failure or during ische
mia could provide new clues for the development of drugs to treat cardiovas
cular diseases. Copyright (C) 1999 S. Karger AG, Basel.