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. 2012 May 10;287(27):22643–22653. doi: 10.1074/jbc.M111.337949

FIGURE 6.

FIGURE 6.

Thrombin-mediated activation of pro-MMP-2 is enhanced by homodimerization of MMP-2. A and B, Western blot analyses of 10 μg/ml pro-MMP-2 incubated with 50 nm thrombin (TH) in COS-1 cells for 4 h using anti-MMP-2 antibody. Prior to these experiments, pro-MMP-2 was purified from the conditioned medium of cells expressing pro-MMP-2 treated with or without PMA (10 ng/ml) or calphostin C (50 nm). The bar graph shows the ratio of activated MMP-2 to pro-MMP-2. Data represent the mean ± S.D. of three experiments. *, p < 0.05 versus the untreated control. IB, immunoblot. C, Western blot analysis of 10 μg/ml pro-MMP-2 incubated with 50 nm thrombin in COS-1 cells for 4 h using anti-MMP-2 antibody. Purified pro-MMP-2 was pretreated with or without calf intestinal alkaline phosphatase (AP; 50 units/ml) at 37 °C for 1 h (n = 2). D, Western blotting of the conditioned medium from cells coexpressing pro-MMP-2 and MT1-MMP treated with or without PMA (10 ng/ml) using anti-MMP-2 antibody (n = 2).