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Isoform‐specific inhibition of voltage‐sensitive Ca 2+ channels by protein kinase C in adrenal chromaffin cells
Author(s) -
Sena Cristina M.,
Santos Rosa M.,
Standen Nick B.,
Boarder Michael R.,
Rosário Luı́s M.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02252-9
Subject(s) - protein kinase c , chromaffin cell , cytosol , phorbol , gene isoform , phospholipase c , endocrinology , medicine , phospholipase a2 , biology , depolarization , protein kinase a , pkc alpha , phospholipase a , microbiology and biotechnology , chemistry , biochemistry , kinase , signal transduction , adrenal medulla , enzyme , catecholamine , gene
Selective protein kinase C (PKC) activators and inhibitors were used to investigate the involvement of specific PKC isoforms in the modulation of voltage‐sensitive Ca 2+ channels (VSCCs) in bovine adrenal chromaffin cells. Exposure to the phorbol ester phorbol‐12,13‐dibutyrate (PDBu) inhibited the Ca 2+ currents elicited by depolarizing voltage steps. This inhibition was occluded by the PKC‐specific inhibitor Ro 31‐8220 but remained unaffected by Gö 6976, a selective inhibitor of conventional PKC isoforms. PDBu treatment caused the translocation of PKC‐α and ‐ϵ isoforms from cytosol to membranes. PKC‐ι and ‐ζ showed no signs of translocation. It is concluded that VSCCs are specifically inhibited by the activation of PKC‐ϵ in chromaffin cells. This may be relevant to the action of phospholipase‐linked receptors involved in the control of Ca 2+ influx, both in catecholaminergic cells and other cell types.