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KMID : 0624620080410120858
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BMB Reports
2008 Volume.41 No. 12 p.858 ~ p.862
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Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity
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Kim Hye-Nan
Chung Hye-Shin
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Abstract
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Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (ΔCT) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the ΔCT MT1-MMP decreased the proMMP-2 activation and inhibited collagen egradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the down-regulation of MT1-MMP activity by promoting internalization from the cell surface.
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KEYWORD
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Caveolin-1, Cell migration, Collagen degradation, MMP-2, MT1-MMP
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