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Cholecystokinin-induced redistribution of paxillin in rat pancreatic acinar cells.

Abstract：

:Cholecystokinin (CCK) dose-dependently stimulates enzyme secretion or loss of cell integrity in the exocrine pancreas. Signaling mechanims include tyrosine phosphorylation of p125(FAK) and paxillin. Here, we examine their potential function. Maximum phosphorylation of both proteins was observed after stimulation of freshly isolated rat pancreatic acini with 10 nM CCK, a concentration known to initiate breakdown of the terminal actin web and cell damage. Under these conditions, CCK initiated transient redistribution of paxillin from the apical cytosol to the apical and lateral plasma membrane within 2 min, where it colocalized with the terminal actin web. Relocation of paxillin was confirmed in subcellular fractions by western blotting and coincided with maximum phosphorylation of membrane-bound p125(FAK) and paxillin. Subsequently, paxillin was redistributed to the basolateral cytosol and was degraded. p125(FAK) remained membrane-bound. We conclude that phosphorylation and redistribution of paxillin and phosphorylation of p125(FAK) may participate in the CCK-induced disassembly of acinar cell actin.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Leser J,Lührs H,Beil MF,Adler G,Lutz MP

doi

10.1006/bbrc.1998.9413

subject

Has Abstract

pub_date

1999-01-19 00:00:00

pages

400-5

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)99413-X

journal_volume

254

pub_type

杂志文章

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