MMP-2: expression, activation and inhibition

Enzyme Protein. 1996;49(1-3):7-19. doi: 10.1159/000468613.


Remodeling of the extracellular matrix (ECM), which occurs during many physiological and pathological processes, is one of the requisite events of cellular invasion. The matrix metalloproteinases (MMPs) are a family of zinc-dependent proteases that are responsible for proteolytic degradation of specific ECM components. Regulating the activity of the MMPs at both mRNA and/or protein levels modulates the degradation of the ECM components which in turn alter cellular invasion. Although most MMPs are regulated via similar mechanisms at the mRNA and protein levels, the modulation of gelatinase A is unique. Understanding the mechanisms that regulate gelatinase A is important since expression and activation of this particular MMP is consistently correlated with a majority of malignant phenotypes. In this report, we will contrast the mechanisms that regulate the expression, activation and inhibition of gelatinase A with the mechanisms that modulate the rest the MMP family.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Enzyme Activation
  • Enzyme Precursors / metabolism
  • Extracellular Matrix / enzymology
  • Gelatinases / antagonists & inhibitors
  • Gelatinases / biosynthesis*
  • Gelatinases / metabolism
  • Glycoproteins / pharmacology
  • Humans
  • Matrix Metalloproteinase 2
  • Metalloendopeptidases / antagonists & inhibitors
  • Metalloendopeptidases / biosynthesis*
  • Metalloendopeptidases / metabolism
  • Protease Inhibitors / pharmacology
  • Proteins / pharmacology
  • Tissue Inhibitor of Metalloproteinase-2
  • Tissue Inhibitor of Metalloproteinases
  • Transcription, Genetic


  • Enzyme Precursors
  • Glycoproteins
  • Protease Inhibitors
  • Proteins
  • Tissue Inhibitor of Metalloproteinases
  • Tissue Inhibitor of Metalloproteinase-2
  • Gelatinases
  • Metalloendopeptidases
  • progelatinase
  • Matrix Metalloproteinase 2