Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions

Pharmacol Ther. 1993 Sep;59(3):329-41. doi: 10.1016/0163-7258(93)90074-n.


The TIMPs play an important role in regulating the activity of the secreted metalloproteinases (collagenases, stromelysins, gelatinases). Two different TIMPS have been well characterized, each capable of inhibiting all tested eukaryotic metalloproteinases but showing specific binding to a particular gelatinase at a site distinct from the active site. They influence the activation of the prometalloproteinase and act to modulate proteolysis of extracellular matrix, notably during tissue remodeling and inflammatory processes. On certain cell types, they can exhibit growth factor-like activity, and they can inhibit the tumorigenic and metastatic phenotype of cancer cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Glycoproteins / analysis
  • Glycoproteins / chemistry
  • Glycoproteins / physiology*
  • Humans
  • Metalloendopeptidases / antagonists & inhibitors*
  • Molecular Sequence Data
  • Neoplasm Metastasis
  • Tissue Inhibitor of Metalloproteinases


  • Glycoproteins
  • Tissue Inhibitor of Metalloproteinases
  • Metalloendopeptidases