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Disruption of angiogenesis by pex, a noncatalytic metalloproteinase fragment with integrin binding activity

Academic Article
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Overview

authors

  • Brooks, P. C.
  • Silletti, S.
  • von Schalscha, T. L.
  • Friedlander, Martin
  • Cheresh, D. A.

publication date

  • February 1998

journal

  • Cell  Journal

abstract

  • Angiogenesis depends on both cell adhesion and proteolytic mechanisms. In fact, matrix metalloproteinase 2 (MMP-2) and integrin alphavbeta3 are functionally associated on the surface of angiogenic blood vessels. A fragment of MMP-2, which comprises the C-terminal hemopexin-like domain, termed PEX, prevents this enzyme binding to alphavbeta3 and blocks cell surface collagenolytic activity. PEX blocks MMP-2 activity on the chick chorioallantoic membrane where it disrupts angiogenesis and tumor growth. Importantly, a naturally occurring form of PEX can be detected in vivo in conjunction with alphavbeta3 expression in tumors and during developmental retinal neovascularization. Levels of PEX in these vascularized tissues suggest that it interacts with endothelial cell alphavbeta3 where it serves as a natural inhibitor of MMP-2 activity, thereby regulating the invasive behavior of new blood vessels.

subject areas

  • Allantois
  • Animals
  • Cell Line
  • Chick Embryo
  • Chorion
  • Collagen
  • Cricetinae
  • Endothelium, Vascular
  • Gelatinases
  • Hemopexin
  • Humans
  • Matrix Metalloproteinase 2
  • Melanoma
  • Metalloendopeptidases
  • Mice
  • Neovascularization, Pathologic
  • Neovascularization, Physiologic
  • Peptide Fragments
  • Protein Binding
  • Receptors, Vitronectin
  • Recombinant Fusion Proteins
  • Retina
  • Retinal Vessels
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80931-9

PubMed ID

  • 9476898
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Additional Document Info

start page

  • 391

end page

  • 400

volume

  • 92

issue

  • 3

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