PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function.

  • Sincock P
  • Fitter S
  • Parton R
 et al. 
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The Transmembrane 4 Superfamily member, PETA-3/CD151, is ubiquitously expressed by endothelial cells in vivo. In cultured human umbilical vein endothelial cells PETA-3 is present on the plasma membrane and predominantly localises to regions of cell-cell contact. Additionally, this protein is abundant within an intracellular compartment which accounts for up to 66% of the total PETA-3 expressed. Intracellular PETA-3 showed colocalisation with transferrin receptor and CD63 suggesting an endosomal/lysosomal localisation which was supported by immuno-electronmicroscopy studies. Co-immunoprecipitation experiments investigating possible interactions of PETA-3 with other molecules demonstrated associations with several integrin chains including beta1, beta3, beta4, (alpha)2, (alpha)3, (alpha)5, (alpha)6 and provide the first report of Transmembrane 4 Superfamily association with the (alpha)6beta4 integrin. Using 2-colour confocal microscopy, we demonstrated similar localisation of PETA-3 and integrin chains within cytoplasmic vesicles and endothelial cell junctions. In order to assess the functional implications of PETA-3/integrin associations, the effect of anti-PETA-3 antibodies on endothelial function was examined. Anti-PETA-3 mAb inhibited endothelial cell migration and modulated in vitro angiogenesis, but had no detectable effect on neutrophil transendothelial migration. The broad range of integrin associations and the presence of PETA-3 with integrins both on the plasma membrane and within intracellular vesicles, suggests a primary role for PETA-3 in regulating integrin trafficking and/or function.

Author-supplied keywords

  • Antigens, CD
  • Antigens, CD151
  • Antigens, CD63
  • Antigens, CD: analysis
  • Antigens, CD: physiology
  • Cell Membrane
  • Cell Membrane: physiology
  • Cell Membrane: ultrastructure
  • Cell Movement
  • Cells, Cultured
  • Endocytosis
  • Endosomes
  • Endosomes: ultrastructure
  • Endothelium, Vascular
  • Endothelium, Vascular: cytology
  • Endothelium, Vascular: physiology
  • Endothelium, Vascular: ultrastructure
  • Humans
  • Integrins
  • Integrins: analysis
  • Intercellular Junctions
  • Intercellular Junctions: physiology
  • Intercellular Junctions: ultrastructure
  • Microscopy, Confocal
  • Microscopy, Immunoelectron
  • Neovascularization, Physiologic
  • Platelet Membrane Glycoproteins
  • Platelet Membrane Glycoproteins: analysis
  • Receptors, Transferrin
  • Receptors, Transferrin: analysis
  • Umbilical Veins

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  • P M Sincock

  • S Fitter

  • R G Parton

  • M C Berndt

  • J R Gamble

  • L K Ashman

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