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Characterization of cAMP‐dependent protein kinase activation by CCK in rat pancreas
Author(s) -
Marino Christopher R.,
Leach Steven D.,
Schaefer Jean F.,
Miller Laurence J.,
Gorelick Fred S.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81734-h
Subject(s) - cholecystokinin , protein kinase a , pde10a , phosphodiesterase , kinase , endocrinology , medicine , chemistry , second messenger system , phosphodiesterase 3 , biology , enzyme , biochemistry , receptor
This study reports on the use of a new sensitive assay of cAMP‐dependent protein kinase activity to examine the effect of cholecystokinin (CCK) on the cAMP second messenger cascade in rat pancreatic acini. Treatment of acini with both low (pM) and high (nM) concentrations of CCK was associated with an increase in cAMP‐dependent protein kinase activity. The increases in kinase activity were detected in the absence of phosphodiesterase inhibition, a condition required to detect a measurable increase in cellular cAMP in these cells. Furthermore, the cAMP cascade was dissociated from the secretory effects of CCK, since the CCK analogue, OPE, mediates enzyme secretion but does not increase cellular cAMP levels or kinase activity.