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Cell surface binding and activation of gelatinase A induced by expression of membrane‐type‐1‐matrix metalloproteinase (MT1‐MMP)
Author(s) -
Sato Hiroshi,
Takino Takahisa,
Kinoshita Takeshi,
Imai Kazushi,
Okada Yasunori,
Stetler Stevenson William G.,
Seiki Motoharu
Publication year - 1996
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 - 10.1016/0014-5793(96)00389-4
Subject(s) - gelatinase a , matrix metalloproteinase , gelatinase , chemistry , cell , metalloproteinase , matrix (chemical analysis) , microbiology and biotechnology , cell membrane , fibroblast activation protein, alpha , biochemistry , biology , genetics , cancer , chromatography
Gelatinase A is secreted as a proenzyme (progelatinase A) which is activated and bound on the surface of tumor and normal cells. We have reported that the expression of a membrane‐type‐1‐matrix metalloproteinase (MT1‐MMP) induces activation of progelatinase A. Here we demonstrate that the expression of MT1‐MMP in COS‐1 cells induces cell‐surface binding of progelatinase A which is consequently processed to an intermediate form. Processing from the intermediate to the fully active form is dependent on the gelatinase A concentration. These results suggest that the cell‐surface binding concentrates the gelatinase A intermediate form locally to allow autoproteolytic processing to the fully active form.