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Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2

Academic Article
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Overview

authors

  • Deryugina, Elena
  • Luo, G. X.
  • Reisfeld, Ralph
  • Bourdon, M. A.
  • Strongin, A.

publication date

  • September 1997

journal

  • Anticancer Research  Journal

abstract

  • We tested the hypothesis that there is a correlation between tumor cell efficiency in activation of matrix metalloproteinase-2 (MMP-2) and invasion through basement membrane-like Matrigel barriers. To generate cells capable of MMP-2 activation, we stably transfected three human tumor cell lines, HT-1080 fibrosarcoma, MCF7 breast carcinoma, and U251.3 glioma with cDNA encoding the full length human membrane-type matrix metalloproteinase-1. Our results show a bimodal correlation between the extent of MMP-2 activation and Matrigel invasion by tumor cells. Cell transfectants characterized by a partial activation of MMP-2 were the most invasive while those with an extensive conversion of MMP-2 proenzyme into enzymatically active forms were the least efficient in invading Matrigel. Modulation of MMP-2 activation by exogenous TIMP-2 reverted the rate of Matrigel invasion by cell transfectants to control levels. We conclude that the regulation of activated MMP-2 in the tumor cells, microenvironment may be critical in facilitating tumor cell invasiveness.

subject areas

  • Collagen
  • Collagenases
  • Drug Combinations
  • Enzyme Activation
  • Gelatinases
  • Humans
  • Integrins
  • Laminin
  • Matrix Metalloproteinase 1
  • Matrix Metalloproteinase 2
  • Metalloendopeptidases
  • Neoplasm Invasiveness
  • Proteoglycans
  • Tissue Inhibitor of Metalloproteinase-2
  • Transfection
  • Tumor Cells, Cultured
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Research

keywords

  • Matrigel
  • cell invasion
  • extracellular matrix
  • matrix metalloproteinase-2
  • membrane-type matrix metalloproteinase-1
  • tissue inhibitor of matrix metalloproteinases-2
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Identity

International Standard Serial Number (ISSN)

  • 0250-7005

PubMed ID

  • 9413149
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Additional Document Info

start page

  • 3201

end page

  • 3210

volume

  • 17

issue

  • 5A

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