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Department of Molecular Virology and Oncology, [T. K., H. S., T. T., M. S.] Cancer Research Institute, Kanazawa University, 13-1 Takaramach, Kanazawa 920 and Department of Analyical Chemistry, [M. I., T. A.] Faculty of Pharmaceutical Science, Setsunan University, 45-I Nagaotoge-cho, Hirakata, Osaka 573-01, Japan
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 Asn66-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.
1 Supported by the Special Coordinating Fund for promoting science and technology from the Ministry of Science and Technology of Japan; by a grant-in-aid from the Ministry of Education, Science, Sports and Culture of Japan; and by the Hokkoku Foundation for Cancer Research.
2 To whom requests for reprints should be addressed, at Cancer Research Institute, Kanazawa University, 13-1 Takamarachi, Kanazawa 920, Japan. Phone: 81-762-34-4504; Fax: 81-762-60-7840; E-mail: vhsato@kenroku.ipc.kanazawa-u.ac.jp.
Received 3/26/96. Accepted 4/30/96.
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