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Papers In Press, published online ahead of print January 7, 2005
Department of Medicine 630-111j, New York Harbor Healthcare System, New York, NY 10010
Corresponding Author: michael.pillinger{at}med.nyu.edu
Since matrix metalloproteinases (MMP) play roles in inflammatory tissue injury, we asked whether MMP secretion by gastric epithelial cells may contribute to gastric injury in response to signals involved in H. pylori-induced inflammation and/or cyclooxygenase inhibition. TNF-
J. Biol. Chem, 10.1074/jbc.M413522200
Submitted on December 1, 2004
Revised on January 7, 2005
Accepted on January 7, 2005
Matrix metalloproteinase secretion by gastric epithelial cells is regulated by E prostaglandins and mitogen-activated protein kinases
, IL-1
and epidermal growth factor (EGF) stimulated gastric cell MMP-1 secretion, indicating that MMP-1 secretion occurs in inflammatory as well as non-inflammatory situations. MMP-1 secretion required activation of the mitogen-activated protein kinase (MAPK) Erk, and subsequent protein synthesis, but was downregulated by the alternate MAPK, p38. In contrast, secretion of MMP-13 was stimulated by TNF-/IL-1 but not EGF, was Erk-independent and mediated by p38. MMP-13 secretion was more rapid (peak 6 h) than MMP-1 (peak = 30 h) and only partly depended on protein synthesis, suggesting initial release of a pre-existing MMP-13 pool. Therefore, MMP-1 and MMP-13 secretion are differentially regulated by MAPKs. MMP-1 secretion was regulated by E prostaglandins (PGEs) in an Erk-dependent manner. PGEs enhanced Erk activation and MMP-1 secretion in response to EGF, but inhibited Erk and MMP-1 when TNF-/IL-1 were the stimuli, indicating that the effects of PGEs on gastric cell responses are context-dependent. These data show that secretion of MMPs is differentially regulated by MAPKs, and suggest mechanisms through which H pylori infection and/or cyclooxygenase inhibition may induce epithelial cell signaling to contribute to gastric ulcerogenesis.
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