Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis

J Biochem. 1996 Feb;119(2):209-15. doi: 10.1093/oxfordjournals.jbchem.a021223.


Activated gelatinase A is reportedly associated with tumor spread. We identified novel matrix metalloproteinases that localize on the cell surface and mediate the activation of progelatinase A. Thus, these progelatinase A activators were named membrane-type matrix metalloproteinase-1 and -2 (MT-MMP-1 and -2, respectively). MT-MMP-1 is overexpressed in malignant tumor tissues, including lung and stomach carcinomas that contain activated gelatinase A. This suggests that MT-MMP-1 is associated with the activation of progelatinase A in these tumor tissues. The expression of MT-MMP-1 also induced binding of gelatinase A to the cell surface by functioning as a receptor. The cell surface localization of proteinases has advantages over pericellular proteolysis. MT-MMP-1 and its family may play a central role in the cell surface localization and activation of progelatinase A and via this mechanism, tumor cell use exogenous progelatinase A to mediate the proteolysis associated with invasion and metastasis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Collagenases / chemistry
  • Collagenases / metabolism*
  • Gelatinases / chemistry
  • Gelatinases / metabolism*
  • Humans
  • Matrix Metalloproteinase 1
  • Matrix Metalloproteinase 2
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / metabolism*
  • Molecular Sequence Data
  • Neoplasm Metastasis*
  • Sequence Homology, Amino Acid


  • Membrane Proteins
  • Collagenases
  • Gelatinases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 1