Evaluation of some newer matrix metalloproteinases

Ann N Y Acad Sci. 1999 Jun 30;878:25-39. doi: 10.1111/j.1749-6632.1999.tb07672.x.

Abstract

Recombinant protein expression techniques have been utilized to facilitate the biochemical and cell biological characterization of human matrix metalloproteinases (MMPs). The importance of the membrane type 1 MMP (MMP 14) in the regulation of pericellular proteolysis, either directly or through the activation of MMP-2, MMP-9, and MMP-13 has been identified. Studies on an in vitro chondrocyte-like cell and an in vivo cartilage repair model indicated that such MT1 MMP-regulated activation cascades are physiologically feasible. MMP19 shows a limited sequence identity with other MMPs and may represent a novel subclass. However, analysis of the recombinant protein identified a number of biochemical properties typical of the MMP family.

Publication types

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

MeSH terms

  • Animals
  • Enzyme Activation
  • Extracellular Matrix / physiology*
  • Humans
  • Matrix Metalloproteinases, Secreted
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism*
  • Models, Biological
  • Recombinant Proteins / metabolism
  • Tissue Inhibitor of Metalloproteinases / pharmacology
  • Tissue Inhibitor of Metalloproteinases / physiology*

Substances

  • Recombinant Proteins
  • Tissue Inhibitor of Metalloproteinases
  • Matrix Metalloproteinases, Secreted
  • Metalloendopeptidases
  • matrix metalloproteinase 19