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Pancreatitis-associated protein I Suppresses NF-κB activation through a JAK/STAT-mediated mechanism in epithelial cells

AuthorsFolch-Puy, Emma ; Granell, Susana; Dagorn, Jean Charles; Iovanna, Juan Lucio; Closa, Daniel
Issue Date15-Mar-2006
PublisherAmerican Association of Immunologists
CitationJournal of Immunology 176(6): 3774-3779 (2006)
AbstractPancreatitis-associated protein I (PAP I), also known as HIP, p23, or Reg2 protein, has recently been implicated in the endogenous regulation of inflammation. Although it was initially characterized as a protein that is overexpressed in acute pancreatitis, PAP I has also been associated with a number of inflammatory diseases, such as Crohn's disease. Knowing thai PAP I and IL-10 responses share several features, we have used a pancreatic acinar cell line (AR42J) to assess the extent to which their expression is reciprocally regulated, and whether the JAK/STAT and NF-κB signaling pathways are involved in the suppression of inflammation mediated by PAP I. We observed that PAP I is induced in epithelial cells by IL-10 and by PAP I itself. In contrast, we found phosphorylation and nuclear translocation of STAT3 and induction of suppressor of cytokine signaling 3 in response to PAP I exposure. Finally, a JAK-speciflc inhibitor, tyrphostin AG490, markedly prevented PAP I-induced NF-κB inhibition, pointing to a cross-talk between JAK/STAT3 and NF-κB signaling pathways. Together, these findings indicate that PAP I inhibits the inflammatory response by blocking NF-κB activation through a STAT3-dependent mechanism. Important functional similarities to the anti-inflammatory cytokine IL-10 suggest that PAP I could play a role similar to that of IL-10 in epithelial cells. Copyright © 2006 by The American Association of Immunologists, Inc.
Identifiersissn: 0022-1767
Appears in Collections:(IIBB) Artículos
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