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. 2014 Aug 1;3(5):1197–1210. doi: 10.1002/cam4.290

Figure 4.

Figure 4

Analysis of recombinant FL-MMP-11 cleavage by recombinant Cat-MMP-14. (A) FL-MMP-11 (FL; 1.9 μmol/L) and Cat-MMP-14 (1.9 μmol/L) proteins were analyzed separately, and after stoichiometric incubation (RT, various times, 12% SDS-PAGE). Silver nitrate staining showed appearance of three main bands after coincubation (F1–F3, black arrowheads). (B) Western blot showed 50% disappearance of FL-MMP-11 after its stoichiometric incubation with Cat-MMP-14 (1.9 μmol/L per MMP, 1 h, RT). Inactive Cat-MMP-14 m had no effect. (C) Kinetic experiment incubating FL-MMP-11 (1.9 μmol/L) with increasing amounts of Cat-MMP-14 (empty arrowheads; 0.1–3.8 μmol/L, 15 min, RT; 12.5–20% gradient SDS-PAGE; silver nitrate). Quantification showed that F1–F3 production increased depending on Cat-MMP-14 quantities. Bands start to appear for 0.1 μmol/L of Cat-MMP-14, and 50% intensity was risen for 0.9–1.9 μmol/L depending on the band observed. (D) In similar experimental conditions (15–12.5% gradient gel), inactive Cat-MMP-14 m had no effect. (A–D) Data from one representative experiment. MMP-14, matrix metalloproteinase-14.