Carbachol activates protein kinase C in dispersed gastric chief cells

We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen...

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Bibliographic Details
Published inBiochemical journal Vol. 300; no. 1; pp. 21 - 24
Main Authors RAFFANIELLO, R. D, RAUFMAN, J.-P
Format Journal Article
LanguageEnglish
Published Colchester Portland Press 15.05.1994
Subjects
Animals
Biological and medical sciences
Carbachol - pharmacology
Cell physiology
Enzyme Activation - drug effects
Fundamental and applied biological sciences. Psychology
Guinea Pigs
Male
Molecular and cellular biology
Pepsinogens - metabolism
Phosphorylation
Protein Kinase C - antagonists & inhibitors
Protein Kinase C - metabolism
Signal transduction
Stomach - cytology
Stomach - enzymology
Tetradecanoylphorbol Acetate - pharmacology
Stomach
Agonist
Protein kinase C
Enzyme
Secretion
Rodentia
Calcium Ions
Pepsinogen
In vitro
Signal transduction
Vertebrata
Mammalia
Guinea pig
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Summary:We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen secretion from dispersed chief cells respectively. Whereas PMA caused a rapid 3-fold increase in peptide kinase activity, carbachol caused a 15% increase in activity that was inhibited by the PKC inhibitor, CGP 41,251. Concentrations of carbamoylcholine and a Ca2+ ionophore that were sub-maximal for stimulation of pepsinogen secretion did not cause PKC activation. These results indicate that, in the absence of PKC activation, other mechanisms, most likely involving changes in cellular Ca2+, are sufficient to stimulate pepsinogen secretion. Nevertheless, carbamoylcholine stimulated maximal secretion of pepsinogen only at concentrations that also resulted in activation of PKC. Moreover, these data indicate that relatively small increases in PKC activity (5-10%) can stimulate pepsinogen secretion from dispersed chief cells.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3000021