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Functional activation of integrin αvβ3 in tumor cells expressing membrane-type 1 matrix metalloproteinase

Academic Article
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Overview

authors

  • Deryugina, Elena
  • Bourdon, M. A.
  • Jungwirth, K.
  • Smith, J. W.
  • Strongin, A. Y.

publication date

  • April 2000

journal

  • International Journal of Cancer  Journal

abstract

  • Matrix metalloproteinases (MMPs) and integrins have been implicated in a variety of processes involved in tumor progression. To evaluate the individual roles of integrin alphavbeta3 and membrane-type 1 matrix metalloproteinase (MT1-MMP), as well as the effects of their joint expression on tumor cell functions, MCF7 breast carcinoma cells were transfected stably with either the MT1-MMP, the beta3 integrin subunit or both MT1-MMP and beta3 cDNAs. MT1-MMP expression is accompanied by the functional activation of integrin alphaVbeta3, thereby increasing vitronectin-mediated adhesion and migration of MCF7 cells transfected with MT1-MMP and integrin alphaVbeta3. MT1-MMP-dependent functional activation of alphaVbeta3 correlates with modification(s) of the beta3 subunit, including its higher electrophoretic mobility and affected the LM609-binding site. MCF7 cells jointly expressing MT1-MMP and alphaVbeta3 were the most efficient in adhesion to the recombinant C-terminal domain of MMP-2 as well as in generating soluble and cell surface associated mature MMP-2 enzyme. These findings suggest a mechanism of selective docking of MMP-2 at tumor cell surfaces, specifically at the sites that include MT1-MMP and activated integrin alphaVbeta3. These mechanisms may provide a link between spatial regulation of focal proteolysis by the cell surface associated MMPs and the regulation of integrin-mediated motility of tumor cells.

subject areas

  • Antigens, CD
  • Binding Sites
  • Breast Neoplasms
  • Cell Adhesion
  • Cell Movement
  • Enzyme Activation
  • Enzyme Precursors
  • Gelatinases
  • Humans
  • Integrin beta3
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases
  • Phenotype
  • Platelet Membrane Glycoproteins
  • Precipitin Tests
  • Receptors, Vitronectin
  • Transfection
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Identity

International Standard Serial Number (ISSN)

  • 0020-7136

Digital Object Identifier (DOI)

  • 10.1002/(sici)1097-0215(20000401)86:1<15::aid-ijc3>3.0.co;2-b

PubMed ID

  • 10728589
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Additional Document Info

start page

  • 15

end page

  • 23

volume

  • 86

issue

  • 1

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