Abstract
Cholecystokinin (CCK) dose-dependently stimulates enzyme secretion or loss of cell integrity in the exocrine pancreas. Signaling mechanims include tyrosine phosphorylation of p125FAKand 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 plasmamembrane 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 p125FAKand paxillin. Subsequently, paxillin was redistributed to the basolateral cytosol and was degraded. p125FAKremained membrane-bound. We conclude that phosphorylation and redistribution of paxillin and phosphorylation of p125FAKmay participate in the CCK-induced disassembly of acinar cell actin.
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