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. 2007 Jun 19;97(2):201–209. doi: 10.1038/sj.bjc.6603856

Figure 2.

Figure 2

Analysis of enzymatic properties of DESC1. (A) Gelatin zymography: purified DESC1 has gelatinolytic activity. Purified GST was used as negative control and 5 μl of the conditioned medium of the cell line HT1080 was used as positive control. ProMMP9 and MMP9, and ProMMP2 and MMP2 gelatinolytic activities are indicated with an arrow. Fibronectin, type I gelatin, laminin and pro-uPA were incubated alone (−) or in presence of purified GST or DESC1. Molecular weight markers (M, kDa) are shown on the left and for pro-uPA, on the right. (B) Fibrinogen was also incubated alone (−) or in presence of GST (lane 2) or DESC1 (lane 3). Preincubation for 30 min at 37°C with 100 μM AEBSF (lane 4), 0.2 mM TPCK (lane 5), 2.5 mM EDTA (lane 6) or 10 μM E64 (lane 7) was carried out before incubation with the substrate. GST and DESC1 positions are indicated on the right. (C) Inhibition assay using the synthetic fluorescent peptide Boc-Gln-Gly-Arg-AMC as susbstrate. Recombinant DESC1 was preincubated in the presence or absence of the protease inhibitors as indicated in Material and Methods. (−) indicates absence of inhibitor.