Human progelatinase A can be activated by matrilysin

FEBS Lett. 1994 May 23;345(1):14-6. doi: 10.1016/0014-5793(94)00412-9.


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.

MeSH terms

  • Amino Acid Sequence
  • Enzyme Activation
  • Enzyme Precursors / drug effects*
  • Enzyme Precursors / genetics
  • Gelatinases / drug effects*
  • Gelatinases / genetics
  • Humans
  • Matrix Metalloproteinase 7
  • Metalloendopeptidases / drug effects*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / pharmacology*
  • Molecular Sequence Data
  • Mutation
  • Protein Processing, Post-Translational
  • Sequence Analysis
  • Substrate Specificity


  • Enzyme Precursors
  • Gelatinases
  • Metalloendopeptidases
  • progelatinase
  • Matrix Metalloproteinase 7