Human progelatinase A can be activated by matrilysin.
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 occurring 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.
Crabbe
T
T
Department of Oncology, Celltech Research, Slough, UK.
Smith
B
B
O'Connell
J
J
Docherty
A
A
D000595:Amino Acid Sequence; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000187:drug effects* / Q000235:genetics; D018093:Gelatinases / Q000187:drug effects* / Q000235:genetics; D006801:Humans; D020783:Matrix Metalloproteinase 7; D008666:Metalloendopeptidases / Q000187:drug effects* / Q000235:genetics / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009154:Mutation; D011499:Protein Processing, Post-Translational; D017421:Sequence Analysis; D013379:Substrate Specificity
D004792:Enzyme Precursors; D018093:Gelatinases; D008666:Metalloendopeptidases; C069860:progelatinase; D020783:Matrix Metalloproteinase 7