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Am J Physiol Gastrointest Liver Physiol 277: G678-G686, 1999;
0193-1857/99 $5.00
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Vol. 277, Issue 3, G678-G686, September 1999

Caerulein-induced NF-kappa B/Rel activation requires both Ca2+ and protein kinase C as messengers

Yusuke Tando, Hana Algül, Martin Wagner, Hans Weidenbach, Guido Adler, and Roland M. Schmid

Department of Medicine I, University of Ulm, 89070 Ulm, Germany

The eukaryotic transcription factor NF-kappa B/Rel is activated by a large variety of stimuli. We have recently shown that NF-kappa B/Rel is induced during the course of caerulein pancreatitis. Here, we show that activation of NF-kappa B/Rel by caerulein, a CCK analog, requires increasing intracellular Ca2+ levels and protein kinase C activation. Caerulein induces a dose-dependent increase of nuclear NF-kappa B/Rel binding activity in pancreatic lobules, which is paralleled by degradation of Ikappa Balpha . Ikappa Bbeta was only slightly affected by caerulein treatment. Consistent with an involvement of Ca2+, the endoplasmic reticulum-resident Ca2+-ATPase inhibitor thapsigargin activated NF-kappa B/Rel in pancreatic lobules. The intracellular Ca2+ chelator TMB-8 prevented Ikappa Balpha degradation and subsequent nuclear translocation of NF-kappa B/Rel induced by caerulein. BAPTA-AM was less effective. Cyclosporin A, a Ca2+/calmodulin-dependent protein phosphatase (PP2B) inhibitor, decreased caerulein-induced NF-kappa B/Rel activation and Ikappa Balpha degradation. The inhibitory effect of bisindolylmaleimide suggests that protein kinase C activity is also required for caerulein-induced NF-kappa B/Rel activation. These data suggest that Ca2+- as well as protein kinase C-dependent mechanisms are required for caerulein-induced NF-kappa B/Rel activation.

pancreas; signaling; acute pancreatitis


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