Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases

Cancer Res. 1992 Feb 1;52(3):701-8.

Abstract

The balance between levels of metalloproteinases and their corresponding inhibitors is a critical factor in tumor invasion and metastasis. Down-regulation of the activity of these proteases was achieved by transfection of invasive and metastatic rat cells with the complementary DNA for metalloproteinase inhibitor/tissue inhibitor of metalloproteinase 2 (MI/TIMP-2), a novel inhibitor of metalloproteinases recently described. (Y. A. DeClerck et al., J. Biol. Chem., 264: 17445-17453, 1989; W. G. Stetler-Stevenson et al., J. Biol. Chem., 264: 17374-17378, 1989). Secretion of functional MI/TIMP-2 protein in stably transfected cells resulted in a marked decrease in metalloproteinase activity. Partial suppression of the formation of lung colonies after i.v. injection in nude mice was observed in a transfected clone expressing high levels of MI/TIMP-2. Production of MI/TIMP-2 in four clones markedly reduced tumor growth rate in vivo after s.c. injection and completely suppressed local tissue invasion. Thus, down-regulation of metalloproteinase activity has a striking effect on local invasion and partially suppresses hematogenous metastasis.

Publication types

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

MeSH terms

  • Animals
  • Genes, ras*
  • Genetic Vectors
  • Glycoproteins / genetics
  • Glycoproteins / metabolism*
  • Humans
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism
  • Mice
  • Mice, Nude
  • Neoplasm Invasiveness / pathology*
  • Neoplasm Metastasis / pathology*
  • Neoplasm Transplantation
  • Neoplasms, Experimental / genetics
  • Neoplasms, Experimental / pathology*
  • Rats
  • Recombinant Proteins / metabolism
  • Restriction Mapping
  • Tissue Inhibitor of Metalloproteinases
  • Transfection*
  • Transplantation, Heterologous

Substances

  • Glycoproteins
  • Recombinant Proteins
  • Tissue Inhibitor of Metalloproteinases
  • Metalloendopeptidases