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Am J Physiol Renal Physiol 280: F628-F635, 2001;
0363-6127/01 $5.00
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Vol. 280, Issue 4, F628-F635, April 2001

Endothelin is a potent inhibitor of matrix metalloproteinase-2 secretion and activation in rat mesangial cells

Jian Yao, Tetsuo Morioka, Bing Li, and Takashi Oite

Department of Cellular Physiology, Institute of Nephrology, Niigata University School of Medicine, Niigata 951 - 8510, Japan

We examined the effects of endothelin (ET) on the activity of matrix metalloproteinase-2 (MMP-2) in cultured MCs. Addition of the ETA receptor antagonists or neutralizing anti-endothelin antibody into MC cultures markedly augmented the secretion and activation of MMP-2. On the contrary, addition of the exogenous ET-1 into MC culture significantly inhibited the synthesis of MMP-2 in both basal and cytokines (tumor necrosis factor-alpha and interferon-gamma ) plus lipopolysaccharide-stimulated conditions. Furthermore, pretreatment of cells with exogenous ET-1 obviously prevented cytochalasin D-elicited activation of MMP-2, an effect that was completely abolished by ETA receptor antagonist, FR139317. In addition, ET-1 was found to be able to suppress the expression of membrane type-1 MMP (MT1-MMP) and promote the conversion of tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) from cell associated form to secreted form. The addition of recombinant TIMP-2 into the culture abrogated dose-dependently the cytochalasin D-elicited activation of MMP-2. These results suggest that ET is a potent inhibitor of MMP-2 secretion and activation in MCs. These novel findings may help us understand the subtle regulation of the synthesis and activation of MMP-2 in MCs. It also provides us with further insight into the pathophysiological mechanisms involving ET in the regulation of matrix turnover in glomerulus.

endothelin receptor antagonist; tissue inhibitor of matrix metalloproteinase-2; zymography; cytochalasin D; cytokines


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