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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

✍ Scribed by Hee-Sook Lee; So-Yun Park; Hyeon Woo Lee; Hye-Seon Choi


Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
261 KB
Volume
92
Category
Article
ISSN
0730-2312

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✦ Synopsis


Abstract

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.