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Am J Physiol Gastrointest Liver Physiol 270: G103-G112, 1996;
0193-1857/96 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 270, Issue 1 103-G112, Copyright © 1996 by American Physiological Society

ARTICLES

Calyculin A, a phosphoprotein phosphatase inhibitor, stimulates acid secretion in isolated gastric glands

T. Urushidani and T. Nagao
Department of Cell Biology, University of Tsukuba, Ibaraki, Japan.

The effects of pkadaic acid (OKA) and calyculin A (CLA), inhibitors of protein phosphatases type 1 (PrPase1) and type 2A (PrPase2A), an acid secretion were examined in rabbit isolated gastric gland, CLA, but not OKA, strongly stimulated acid secretion by itself without affecting glandular adenosine 3',5'-cyclic monophosphate (cAMP) contents. CLA-induced secretion was suggested to be mainly due to the increase in the phosphorylation of protein kinase A substrates via the inhibition of PrPase1 in the parietal cell, since 1) CLA-induced secretion was not inhibited by cimetidine or atropine, 2) a protein kinase A inhibitor inhibited the secretion, whereas a protein kinase C inhibitor did not, 3) CLA augmented dibutyryl cAMP-induced secretion in some cases, and 4) OKA, which is 100 times more selective to PrPase2A than to PrPase1, was not a secretagogue. Unexpectedly, CLA did not augment the secretion by histamine, possibly because the inhibitor augmented the phosphorylation-mediating negative feedback pathway as well. Both CLA and OKA markedly increased phosphorylation of ezrin, a putative protein kinase A substrate, in the course of secretory activation.


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