August 1994
Volume 35, Issue 9
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Articles  |   August 1994
Vasculotropin-VEGF stimulates retinal capillary endothelial cells through an autocrine pathway.
Author Affiliations
  • V Simorre-Pinatel
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • M Guerrin
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • P Chollet
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • M Penary
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • S Clamens
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • F Malecaze
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
  • J Plouet
    Laboratoire de Biologie Moléculaire Eucaryote, Laboratoire d'Ophtalmologie, CHU, Toulouse, France.
Investigative Ophthalmology & Visual Science August 1994, Vol.35, 3393-3400. doi:
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      V Simorre-Pinatel, M Guerrin, P Chollet, M Penary, S Clamens, F Malecaze, J Plouet; Vasculotropin-VEGF stimulates retinal capillary endothelial cells through an autocrine pathway.. Invest. Ophthalmol. Vis. Sci. 1994;35(9):3393-3400.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

PURPOSE: To determine whether bovine retinal endothelial cells (BRECs) bind, synthesize, and respond to vasculotropin-vascular endothelial growth factor (VAS-VEGF). METHODS: Cultured BRECs were tested for their ability to bind 125I VAS-VEGF and their response to the growth and migration-promoting effect of VAS-VEGF. Total RNAs extracted from BRECs were reverse transcribed and amplified by polymerase chain reaction using VAS-VEGF primers. The translation was assessed by a Western blot analysis and a radioreceptor assay in the BREC-conditioned medium. Neutralization with anti-VAS-VEGF antibodies ascertained the autocrine role of VAS-VEGF. RESULTS: BRECs bind VAS-VEGF on two high-affinity binding sites (apparent Kd of 2 and 56 pM) and can proliferate and migrate upon the addition of recombinant VAS-VEGF. Furthermore, BRECs synthesize and secrete into their own culture medium a mitogen related to VAS-VEGF as far as two factors are concerned: chromatographic behavior on heparin-affinity columns, and cross-reactivity with recombinant VAS-VEGF to the binding to its receptors or antibodies. Neutralization of the purified conditioned medium with anti-VAS-VEGF antibodies revealed that VAS-VEGF can act on BRECs through an autocrine pathway. CONCLUSIONS: This is the first description of an autocrine regulation of endothelial cell growth by VAS-VEGF that could be involved in the pathogenesis of retinal neovascularization.

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