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Loss of p53 compensates for alpha(v)-integrin function in retinal neovascularization

Academic Article
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Overview

authors

  • Stromblad, S.
  • Fotedar, A.
  • Brickner, H.
  • Theesfeld, C.
  • de Diaz, E. A.
  • Friedlander, Martin
  • Cheresh, D. A.

publication date

  • April 2002

journal

  • Journal of Biological Chemistry  Journal

abstract

  • alpha(v)-Integrin antagonists block neovascularization in various species, whereas 20% of alpha(v)-integrin null mice are born with many normal looking blood vessels. Given that blockade of alpha(v)-integrins during angiogenesis induces p53 activity, we utilized p53 null mice to elucidate whether loss of p53 can compensate for alpha(v)-integrin function in neovascularization of the retina. Murine retinal vascularization was inhibited by systemic administration of an alpha(v)-integrin antagonist. In contrast, mice lacking p53 were refractory to this treatment, indicating that neovascularization in normal mice depends on alpha(v)-integrin-mediated suppression of p53. Blockade of alpha(v)-integrins during neovascularization resulted in an induction of p21(CIP1) in wild type and, surprisingly, in p53 null retinas, indicating that alpha(v)-integrin ligation regulates p21(CIP1) levels in a p53-independent manner. In conclusion, we demonstrate for the first time an in vivo intracellular mechanism for compensation of integrin function and that p53 and alpha(v)-integrins act in concert during retinal neovascularization.

subject areas

  • Animals
  • Antigens, CD
  • Blotting, Western
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins
  • Dose-Response Relationship, Drug
  • Genotype
  • Heterozygote
  • Integrin alphaV
  • Mice
  • Mice, Knockout
  • Microscopy, Fluorescence
  • Models, Biological
  • Neovascularization, Physiologic
  • Protein Binding
  • Retina
  • Signal Transduction
  • Tumor Suppressor Protein p53
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.C200044200

PubMed ID

  • 11856728
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Additional Document Info

start page

  • 13371

end page

  • 13374

volume

  • 277

issue

  • 16

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