Membrane-type matrix metalloproteinases

APMIS. 1999 Jan;107(1):137-43. doi: 10.1111/j.1699-0463.1999.tb01536.x.

Abstract

Matrix metalloproteinases (MMP) degrade components of extracellular matrix (ECM), and thereby regulate formation, remodeling and maintenance of tissue. Abnormal function of cell surface proteases associated with malignant tumors may contribute directly to the invasive and malignant nature of the cells. Among the MMP's associated with the tumor cell surface, gelatinase A is believed to be particularly important, since it degrades type IV collagen, and is activated in a tumor specific manner, correlating with tumor spread and poor prognosis. Activation of pro-gelatinase A is uniquely regulated by a cell-mediated mechanism. This study describes an in vitro model that mimics the cell-surface activation mechanism. The expression of MT-MMP could not be detected in normal epithelial cells, but can be seen in transformed epithelial carcinoma cells.

Publication types

  • Review

MeSH terms

  • Animals
  • Enzyme Activation
  • Enzyme Precursors / physiology
  • Gelatinases / physiology
  • Humans
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / physiology*
  • Neoplasm Invasiveness
  • Transcription, Genetic

Substances

  • Enzyme Precursors
  • Gelatinases
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases
  • progelatinase