Human progelatinase A can be activated by matrilysin
- 23 May 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 345 (1) , 14-16
- https://doi.org/10.1016/0014-5793(94)00412-9
Abstract
The activation of human progelatinase A by other matrix metalloproteinases was studied by following both the loss of its N-terminal propeptide and the accompanying increase in the rate of hydrolysis of a synthetic substrate. Activated stromelysin 1 was unable to cause any activation of progelatinase A beyond that slowly occuring by autolysis, but an 8 h incubation with activated matrilysin was able to produce 64% of the activity generated by incubation with (4-aminophenylmercuric)acetate (APMA). Wild-type progelatinase A and a mutant proenzyme that cannot become active were both cleaved by matrilysin to a lower molecular weight species that had lost the propeptide. This shows that matrilysin activates progelatinase A by removing the propeptide in a process that does not require any autolytic cleavages.Keywords
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