Characterization of cAMP‐dependent protein kinase activation by CCK in rat pancreas

FEBS Letters

Miller, Laurence J.²  Gorelick, Fred S.¹  Leach, Steven D.¹  Marino, Christopher R.¹  Schaefer, Jean F.¹ 

[1] Departments of Medicine and Surgery, West Haven VA Medical Center and Yale University School of Medicine, 333 Cedar St., New Haven, CT 06510, USA;Gastroenterology Basic Research Unit, Mayo Clinic, 200 First St. SW, Rochester, MN 55905, USA

关键词: Pancreatic acini;    Cholecystokinin;    CCK receptor;    Adenosine 3′;    5′ cyclic monophosphate;    Protein kinase;    Phosphodiesterase inhibitor;    CCK;    cholecystokinin octapeptide;    OPE;    d-Tyr-Gly-[(Nle 28.31)CCK-26-32]-phenethyl ester;    cAMP;    adenosine 3′;    5′ cyclic monophosphate;    IBMX;    3-isobutyl-1-methylxanthine.;   

DOI  :  10.1016/0014-5793(93)81734-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown