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Am J Physiol Gastrointest Liver Physiol 282: G450-G460, 2002; doi:10.1152/ajpgi.00042.2001
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Vol. 282, Issue 3, G450-G460, March 2002

Caspase 8-mediated cleavage of plectin precedes F-actin breakdown in acinar cells during pancreatitis

Michael Beil1, Jürgen Leser1, Manfred P. Lutz1, Anna Gukovskaya2, Thomas Seufferlein1, Grit Lynch1, Stephen J. Pandol2, and Guido Adler1

1 Department of Internal Medicine I, University of Ulm, 89070 Ulm, Germany; and 2 Veterans Affairs Greater Los Angeles Healthcare System, University of California, Los Angeles, California 90073

Pancreatic acinar cells depend on the integrity of the cytoskeleton for regulated secretion. Stimulation of isolated rat pancreatic acini with the secretagogue CCK serves as a model for human acute edematous pancreatitis. It induces the breakdown of the actin filament system (F-actin) with the consecutive inhibition of secretion and premature activation of digestive enzymes. However, the mechanisms that regulate F-actin breakdown are largely unknown. Plectin is a versatile cytolinker protein regulating F-actin dynamics in fibroblasts. It was recently demonstrated that plectin is a substrate of caspase 8. In pancreatic acinar cells, plectin strongly colocalizes with apical and basolateral F-actin. Supramaximal secretory stimulation of acini with CCK leads to a rapid redistribution and activation of caspase 8, followed by degradation of plectin that in turn precedes the F-actin breakdown. Inhibition of caspase 8 before CCK hyperstimulation prevents plectin cleavage, stabilizes F-actin morphology, and reverses the inhibition of secretion. Thus we propose that the caspase 8-mediated degradation of plectin represents a critical biochemical event during CCK-induced secretory blockade and cell injury.

cholecystokinin; cytoskeleton; pancreas; secretion


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