Proteases Associated With Invadopodia, and Their Role in Degradation of Extracellular Matrix

Enzyme Protein. 1996;49(1-3):59-71. doi: 10.1159/000468616.

Abstract

Metastasizing cancer cells invade the extracellular matrix using plasma membrane protrusions (invadopodia) that contact and dissolve the matrix. Evidence suggests that membrane-associated proteases, 170-kD gelatinase (seprase) and Gelatinase A, exert their mechanisms of action on invadopodia. Potential roles that other metallo- and serine-types of membrane proteases, including membrane-type matrix metalloprotease, meprin, dipeptidyl peptidase IV, fibroblast activation protein alpha and guanidinobenzoatase, play in the cell surface proteolysis are also discussed. It is proposed that formation of a structurally and functionally linked protease complex on invadopodia allows the invasion of cancer cells into the extracellular matrix.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Dipeptidyl Peptidase 4 / metabolism
  • Endopeptidases / metabolism*
  • Enzyme Activation
  • Extracellular Matrix / enzymology*
  • Gelatinases / metabolism
  • Humans
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinases, Membrane-Associated
  • Membrane Proteins / metabolism
  • Metalloendopeptidases / metabolism
  • Molecular Weight
  • Neoplasm Invasiveness
  • Neoplasm Metastasis / pathology*
  • Serine Endopeptidases / metabolism
  • Tiopronin / metabolism

Substances

  • Membrane Proteins
  • Tiopronin
  • Endopeptidases
  • Dipeptidyl Peptidase 4
  • Serine Endopeptidases
  • fibroblast activation protein alpha
  • Gelatinases
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2