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J Biol Chem, Vol. 274, Issue 2, 735-738, January 8, 1999
From the Howard Hughes Medical Institute and the Department of
Molecular Physiology and Biophysics, Vanderbilt University School of
Medicine, Nashville, Tennessee 37232-0295
Phospholipase D (PLD) has been implicated in
vesicle trafficking in the Golgi and hence secretion. In this study, we
show that the secretion of matrix metalloproteinase-9 (MMP-9) from HT
1080 human fibrosarcoma cells was stimulated by phorbol 12-myristate 13-acetate in a time- and dose-dependent manner that
involved protein kinase C. The phorbol ester also increased PLD
activity in the cells. Evidence that PLD was involved in the
stimulation of MMP-9 secretion was provided by the observations that
the secretion of MMP-9 was stimulated by the introduction of
short-chain phosphatidic acid (PA) into the growth medium and that
inhibition of PA production by 1-propanol inhibited secretion. Using a
short-chain diacylglycerol we excluded the possibility that MMP-9
secretion was induced by diacylglycerol formed from PA by phosphatidic
acid phosphatase. Furthermore, propranolol, an inhibitor of this
enzyme, had no effect on secretion induced by either phorbol
12-myristate 13-acetate or PA. The data presented here indicate that
activation of protein kinase C increases MMP-9 secretion in HT 1080 cells and implicate PLD and PA formation in the effect.
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