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Am J Physiol Cell Physiol 267: C1224-C1230, 1994;
0363-6143/94 $5.00
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AJP - Cell Physiology, Vol 267, Issue 5 C1224-C1230, Copyright © 1994 by American Physiological Society

ARTICLES

Protein kinase C activity does not mediate the inhibitory effect of carbachol on chloride secretion by T84 cells

A. E. Traynor-Kaplan, T. Buranawuti, M. Vajanaphanich and K. E. Barrett
Department of Medicine, School of Medicine, University of California, San Diego 92103.

Carbachol induces calcium-dependent chloride secretion and activates protein kinase C in T84 cells. However, prolonged stimulation with carbachol or direct activation of protein kinase C inhibits subsequent calcium-dependent chloride secretion. Furthermore, the ability of carbachol to elevate inositol tetrakisphosphate levels may be linked to inhibition of chloride secretion. Here we demonstrate that protein kinase C activation increases levels of inositol tetrakisphosphates (1,3,4,6- and 3,4,5,6-isomers) in T84 colonic epithelia. Furthermore, this corresponds to an inhibition of chloride secretion. However, protein kinase C is unlikely to mediate the analogous effects of carbachol. Neither the ability of carbachol to inhibit calcium-dependent chloride secretion nor its effects on inositol 3,4,5,6-tetrakisphosphate levels were reversed by staurosporine. Carbachol also has quantitatively and qualitatively different effects on inositol tetrakisphosphate isomers than protein kinase C activators. Thus protein kinase C activity can increase levels of various inositol tetrakisphosphate isomers within T84 cells but does not mediate carbachol-induced increases in these putative messengers. These data further support the hypothesis that inositol 3,4,5,6-tetrakisphosphate is a negative second messenger, uncoupling epithelial chloride secretion from changes in intracellular calcium.


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