The recombinant catalytic domain of membrane‐type matrix metalloproteinase‐1 (MT1‐MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP‐2

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Abstract
A truncated form of the membrane‐type matrix metalloproteinase‐1 [(Ala21‐Ile318)proMT1‐MMP] lacking the hemopexin‐like and trans‐membrane domain was produced in E. coli. We demonstrate that the recombinant proenzyme was autoproteolytically processed to a fully active catalytic domain with N‐terminal Ile114. The catalytic domain of MT1‐MMP initiated the activation of progelatinase A and progelatinase A complexed with tissue inhibitor of metalloproteinases‐2 (TIMP‐2). As a typical soluble metalloproteinase it was able to cleave physiologic as well as synthetic substrates. Our kinetic data demonstrate that TIMP‐2 is a potent inhibitor for the recombinant enzyme.