SECRETION OF MMP-9 BY SOLUBLE GLUCOCORTICOID-INDUCED TUMOR NECROSIS FACTOR RECEPTOR (SGITR) IS MEDIATED BY PHOSPHOLIPASE D (PLD) IN MURINE MACROPHAGE

摘要

Secretion of matrix matalloproteinase (MMP-9) is stimulated by glucocorticoid induced tumor necrosis factor receptor (GITR), a new TNFR family, in murine macrophages via activation of phospholipase D (PLD). PLD has been implicated in secretion involved in vesicle trafficking of the Golgi complex. Secretion of MMP-9 is stimulated by the phosphatidic acid and inhibition of phosphatidic acid production by 1-propanol inhibited secretion of MMP-9 by soluble GITR (sGITR). MMP-9 is not produced by diacylglycerol and an inhibitor of phosphatidic acid phosphatase has no effect on secretion induced by sGITR, indicating that phosphatidic acid is responsible for MMP-9 secretion in murine macrophages. Our data indicates that activation of PKC delta increases MMP-9 secretion in macrophages stimulated by sGITR and PLD is involved in the process.