The specific phosphatase inhibitor, Calyculin-A (CL-A), decreases high
-K stimulated catecholamine secretion in bovine chromaffin cells. This
effect can be split into two components: one needs long exposures to
the drug to be elicited, and is sensitive to the protein kinase-inhibi
tor K252a; the other is observed after short incubations of CL-A, and
is insensitive to K252a. Here we report that the latter component is d
ue to an external block, by CL-A, of chromaffin cell calcium channels
in a voltage-dependent, reversible and phosphorylation-independent man
ner.