| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI, USA
* To whom correspondence should be addressed. E-mail: clzmli{at}umich.edu.
Protein kinase C (PKC) is known to be activated by pancreatic secretagogues such
as cholecystokinin (CCK) and carbachol, and to participate along with calcium in
amylase release. Four PKC isoforms, alpha (
), delta (
), epsilon (
) and zeta (
), have
been identified in acinar cells, but which isoforms participate in amylase release are
unknown. To identify the responsible isoforms, we used translocation assays, chemical
inhibitors and overexpression of individual isoforms and their dominant negative variants
by means of adenoviral vectors. CCK stimulation caused translocation of PKC , and ,
but not from soluble to membrane fraction. CCK-induced amylase release was
inhibited about 30 % by GF109203X, a broad spectrum PKC inhibitor, and by rottlerin, a
PKC inhibitor, but not by Go6976, a PKC inhibitor, at concentrations from 1 to 5
µM. Neither overexpression of wild type or dominant-negative PKC affected CCK-induced
amylase release. Overexpression of PKC and enhanced amylase release,
while only dominant negative PKC inhibited amylase release by 25 %. PKC
overexpression increased amylase release at all concentrations of CCK, but dominant
negative PKC only inhibited the maximal concentration; both similarly affected
carbachol and JMV-180-induced amylase release. Overexpression of both PKC and its
dominant negative variant affected the late but not the early phase of amylase release.
GF109203X totally blocked the enhancement of amylase release by PKC , but had no
further effect in the presence of dominant negative PKC . These results indicate that
PKC is the PKC isoform involved with amylase secretion.
This article has been cited by other articles:
|
|
 |
|
  E. C. Thrower, S. Osgood, C. A. Shugrue, T. R. Kolodecik, A. M. Chaudhuri, J. R. Reeve Jr, S. J. Pandol, and F. S. Gorelick The novel protein kinase C isoforms -{delta} and -{varepsilon} modulate caerulein-induced zymogen activation in pancreatic acinar cells Am J Physiol Gastrointest Liver Physiol, June 1, 2008; 294(6): G1344 - G1353. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. I. Cosen-Binker, P. P. L. Lam, M. G. Binker, J. Reeve, S. Pandol, and H. Y. Gaisano Alcohol/Cholecystokinin-evoked Pancreatic Acinar Basolateral Exocytosis Is Mediated by Protein Kinase C{alpha} Phosphorylation of Munc18c J. Biol. Chem., April 27, 2007; 282(17): 13047 - 13058. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Satoh, A. S. Gukovskaya, J. R. Reeve Jr, T. Shimosegawa, and S. J. Pandol Ethanol sensitizes NF-{kappa}B activation in pancreatic acinar cells through effects on protein kinase C-{epsilon} Am J Physiol Gastrointest Liver Physiol, September 1, 2006; 291(3): G432 - G438. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Dufresne, C. Seva, and D. Fourmy Cholecystokinin and gastrin receptors. Physiol Rev, July 1, 2006; 86(3): 805 - 847. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |
