Proteases and their inhibitors in human brain tumours: a review

Anticancer Res. Nov-Dec 1997;17(6B):4151-62.

Abstract

Proteases such as matrix metalloproteinases (MMPs), cysteine- and serine-proteinases are capable of degrading extracellular matrix and basement membranes and have been implicated in human brain tumours. MMPs are a homologous family of zinc-dependent proteases. Within this group, attention has been focused on the gelatinases (MMP-2 and MMP-9) which are thought to play an important role in tumour progression. The cysteine proteinases which have received most attention in relation to tumour progression are cathepsin B (CB) and to a lesser extent cathepsin L (CL). Among the serine proteinases, urokinase plasminogen activator and its receptor have been the subject of much investigation. In the present review, evidence from current literature on the possible role or significance of serine- and cysteine-proteinases and MMPs and their inhibitors in human brain tumours is discussed with special reference to gliomas. Although direct evidence is reported for MMPs and serine proteinases to support their role in glioma invasion, much of the evidence for the involvement of cysteine proteinases remains circumstantial.

Publication types

  • Review

MeSH terms

  • Brain Neoplasms / enzymology*
  • Brain Neoplasms / physiopathology
  • Cell Movement / physiology
  • Cysteine Endopeptidases / metabolism
  • Cysteine Endopeptidases / physiology
  • Endopeptidases / metabolism*
  • Extracellular Matrix / physiology
  • Humans
  • Metalloendopeptidases / antagonists & inhibitors
  • Metalloendopeptidases / metabolism
  • Neoplasm Invasiveness
  • Protease Inhibitors / pharmacology*
  • Serine Endopeptidases / metabolism
  • Serine Endopeptidases / physiology
  • Tissue Inhibitor of Metalloproteinases / metabolism*
  • Tissue Inhibitor of Metalloproteinases / physiology

Substances

  • Protease Inhibitors
  • Tissue Inhibitor of Metalloproteinases
  • Endopeptidases
  • Serine Endopeptidases
  • Cysteine Endopeptidases
  • Metalloendopeptidases