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Direct production of an activated matrix metalloproteinase‐9 (gelatinase B) from mammalian cells
Author(s) -
Watanabe Yoshifumi,
Hirakawa Koichiro,
Haruyama Takahiro,
Akaike Toshihiro
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02664-3
Subject(s) - furin , matrix metalloproteinase , transfection , gelatinase , metalloproteinase , gelatinase a , mutant , in vitro , chemistry , microbiology and biotechnology , collagenase , biochemistry , gene , biology , enzyme
Matrix metalloproteinase‐9 (MMP‐9) is produced by the inactive proform and activated by a proteolytic process. However, it has not been reported to produce the active form directly from cells, which has hindered the research to elicit the physiological roles of this enzyme. In this study, we prepared mutant MMP‐9 containing the furin‐recognizing sequence in the prodomain and showed that the mutant MMP‐9 was secreted as the active form directly from CHO‐K1 cells and primary hepatocytes after the gene was transfected. The secreted MMP‐9 showed proteolytic activity without further activation and degraded collagen IV in vitro. In addition, the transfection of the gene into the liver resulted in the efficient expression of active MMP‐9 in the liver and the serum in vivo.