Please use this identifier to cite or link to this item: http://hdl.handle.net/10316/3888
Title: Isoform-specific inhibition of voltage-sensitive Ca2+ channels by protein kinase C in adrenal chromaffin cells
Authors: Sena, Cristina M. 
Santos, Rosa M. 
Standen, Nick B. 
Boarder, Michael R. 
Rosário, Luís M. 
Keywords: Protein kinase C; Voltage-sensitive Ca2+ channel; Adrenal chromaffin cell; Phorbol-12,13-dibutyrate; Ro 31-8220; Gö 6976
Issue Date: 2001
Citation: FEBS Letters. 492:1-2 (2001) 146-150
Abstract: Selective protein kinase C (PKC) activators and inhibitors were used to investigate the involvement of specific PKC isoforms in the modulation of voltage-sensitive Ca2+ channels (VSCCs) in bovine adrenal chromaffin cells. Exposure to the phorbol ester phorbol-12,13-dibutyrate (PDBu) inhibited the Ca2+ 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-[alpha] and -[epsilon] isoforms from cytosol to membranes. PKC-[iota] and -[zeta] showed no signs of translocation. It is concluded that VSCCs are specifically inhibited by the activation of PKC-[epsilon] in chromaffin cells. This may be relevant to the action of phospholipase-linked receptors involved in the control of Ca2+ influx, both in catecholaminergic cells and other cell types.
URI: http://hdl.handle.net/10316/3888
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

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