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- W1964550340 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." @default.
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- W1964550340 date "1994-05-23" @default.
- W1964550340 modified "2023-10-14" @default.
- W1964550340 title "Human progelatinase A can be activated by matrilysin" @default.
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- W1964550340 doi "https://doi.org/10.1016/0014-5793(94)00412-9" @default.
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