Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M
Department of Molecular Virology and Oncology, Cancer Research Institute, Kanazawa University, Japan.
Cancer Res. 1996 Jun 1;56(11):2535-8.
Membrane-type 1 matrix metalloproteinase that is associated with the proteolytic activation of progelatinase A was expressed as a recombinant fusion protein in Escherichia coli. The recombinant enzyme cleaved the propeptide sequence of gelatinase A in a sequence-specific manner. A mutant progelatinase A that has a substitution of Asn(66)-Leu to Ile-Val was not processed at all. The processing was blocked by tissue inhibitor of metalloproteinases-2 or BB-94 but not by tissue inhibitor of metalloproteinases-1. Thus, membrane-type 1 matrix metalloproteinase is a direct activator of progelatinase A without requiring additional proteases.
与前明胶酶A的蛋白水解激活相关的膜型1基质金属蛋白酶在大肠杆菌中表达为重组融合蛋白。重组酶以序列特异性方式切割明胶酶A的前肽序列。一种将Asn(66)-Leu替换为Ile-Val的突变型前明胶酶A根本没有被加工。这种加工被金属蛋白酶组织抑制剂-2或BB-94阻断，但不被金属蛋白酶组织抑制剂-1阻断。因此，膜型1基质金属蛋白酶是前明胶酶A的直接激活剂，无需额外的蛋白酶。
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