Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis
J. Clin. Invest. Michael P. Herman, et al. 107:1117 doi:10.1172/JCI10403 [Go to this article.]

Figure 2
TFPI-2 inhibits processing of triple-helical type I collagen (Col I) by interstitial collagenases. Purified human triple-helical type I collagen (100 μg/ml) was incubated (24 hours, 25°C) with either MMP-1 (a) or MMP-13 (b) (both at 10 μg/ml) preincubated with the respective concentration of TFPI-2 or TIMP-1, or (c) incubated with MMP-1 and MMP-13 (both at 10 μg/ml) preincubated with TFPI-2 (100 μg/ml) complexed (45 minutes, 37°C) with VIIa/TF (20 nM). Reactions were applied to Western blot analysis with anti–type I collagen Ab. (d) Human recombinant MMP-1 or MMP-13 (both at 10 μg/ml) were incubated with TFPI-2 (100 μg/ml) complexed with the respective concentrations of VIIa/TF, and the subsequent ability of the MMPs to process native fluorogenic substrate was measured as described. Percentage of activity was normalized to the activity obtained with the respective MMP lacking TFPI-2. Data shown represent mean ± SD and are representative of at least three independent experiments.