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Calcium induces rapid changes in protein phosphorylation in permeabilized pancreatic acini.

Authors
  • Wagner, A C
  • Williams, J A
Type
Published Article
Journal
Pancreas
Publisher
Ovid Technologies (Wolters Kluwer) - Lippincott Williams & Wilkins
Publication Date
Oct 01, 1995
Volume
11
Issue
3
Pages
236–240
Identifiers
PMID: 8577676
Source
Medline
License
Unknown

Abstract

Calcium is an important mediator of pancreatic stimulus-secretion coupling, and in streptolysin O-permeabilized acini maximal amylase release can be induced by 1 microMCa2+. Two-dimensional analysis of acinar phosphoproteins using 32P-labeled acini showed that 1-min stimulation of permeabilized acini with 1 microMCa2+ induced a number of rapid protein phosphorylation and dephosphorylation events similar to previously observed effects of secretagogues acting on intact acini. The rapid Ca2+ effects on protein phosphorylation correlated well with the earliest detectable onset of amylase release after 1 min of incubation with Ca2+. Our findings indicate that some of the agonist-induced changes in protein phosphorylation are mediated by Ca2+ and also provide evidence for the possible involvement of Ca(2+)-mediated dephosphorylation in acinar stimulus-secretion coupling.

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