Cell surface binding and activation of gelatinase A induced by expression of membrane‐type‐1‐matrix metalloproteinase (MT1‐MMP)
H Sato, T Takino, T Kinoshita, K Imai, Y Okada… - FEBS …, 1996 - Wiley Online Library
FEBS letters, 1996•Wiley Online Library
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 …
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 …
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.
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