Src Kinase Pathways in Extracellular Ca 2+ -Dependent Pancreatic Enzyme Secretion

Authors: Tsunoda Y.; Yoshida H.; Africa L.; Steil G.J.; Owyang C.

Source: Biochemical and Biophysical Research Communications, Volume 227, Number 3, October 1996 , pp. 876-884(9)

Publisher: Academic Press

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Abstract:

We investigated the functional roles of Src kinase pathways in rat pancreatic acinar cells. CCK-8 dose-dependently increased Src kinase activities by a mechanism that was sensitive to herbimycin A. CCK-8 enhanced protein tyrosine kinase (PTK) activities when the synthetic Src peptide was used as a substrate. Increased PTK activities, sustained Ca 2+ entry, and amylase secretion, all stimulated by CCK-8, were abolished by eliminating extracellular Ca 2+ ([Ca 2+ ] o ). CCK-8 caused tyrosine phosphorylation of three major proteins: 60 KDa, 85 KDa, and 105 KDa. The elimination of [Ca 2+ ] o prevented the tyrosine phosphorylations of p60 and p105, but not p85. Therefore, the p60 Src kinase and the p105 kinase, referred to as `Src kinase kinase', may be involved in [Ca 2+ ] o -dependent pancreatic exocytosis.

Language: English

Document Type: Research article

Affiliations: Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan, 48109-0682:

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