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Secretions of MMP‐9 by soluble glucocorticoid‐induced tumor necrosis factor receptor (sGITR) mediated by protein kinase C (PKC)δ and phospholipase D (PLD) in murine macrophage
Author(s) -
Lee HeeSook,
Park SoYun,
Lee Hyeon Woo,
Choi HyeSeon
Publication year - 2004
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20099
Subject(s) - protein kinase c , phosphatidic acid , phospholipase d , diacylglycerol kinase , secretion , tumor necrosis factor alpha , endocrinology , biology , chemistry , microbiology and biotechnology , medicine , kinase , signal transduction , biochemistry , phospholipid , membrane
The secretion of matrix metalloproteinase (MMP‐9) is stimulated by the glucocorticoid‐induced tumor necrosis factor receptor (GITR), a new tumor necrosis factor receptor (TNFR) family, in murine macrophages via an activation of protein kinase C (PKC)δ and phospholipase D (PLD). Secretions of MMP‐9 are stimulated by the phosphatidic acid (PA), a product of PLD activity and an inhibition of PA production by a 1‐propanol inhibited secretion of MMP‐9 by soluble GITR (sGITR). MMP‐9 is not secreted by diacylglycerol (DAG) and an inhibitor of PA phosphatase has no effect on the secretion induced by sGITR, indicating that PA is responsible for MMP‐9 secretion in murine macrophages. Our data indicates that sGITR‐induced activation of PKCδ and PLD increases MMP‐9 secretions in macrophages. © 2004 Wiley‐Liss, Inc.