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Human progelatinase A can be activated by matrilysin
Author(s) -
Crabbe Thomas,
Smith Bryan,
O'Connell James,
Docherty Andrew
Publication year - 1994
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(94)00412-9
Subject(s) - matrilysin , autolysis (biology) , chemistry , matrix metalloproteinase , incubation , substrate (aquarium) , protein precursor , mutant , substrate specificity , biochemistry , enzyme , biology , gene , ecology
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.