Please use this identifier to cite or link to this item:
https://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: | https://hdl.handle.net/10316/3888 | DOI: | 10.1016/S0014-5793(01)02252-9 | Rights: | openAccess |
Appears in Collections: | FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
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