Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/8940
Type: Journal article
Title: 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
Author: Sincock, P.
Fitter, S.
Parton, R.
Berndt, M.
Gamble, J.
Ashman, L.
Citation: Journal of Cell Science, 1999; 112(6):833-844
Publisher: Company of Biologists
Issue Date: 1999
ISSN: 0021-9533
1477-9137
Statement of
Responsibility: 
Paul M. Sincock, Stephen Fitter, Robert G. Parton, Michael C. Berndt, Jennifer R. Gamble and Leonie K. Ashman
Abstract: 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.
Keywords: TM4SF; Integrin; Cell migration; Multi-protein complex; Protein trafficking; Angiogenesis
RMID: 0030004894
Published version: http://jcs.biologists.org/cgi/content/abstract/112/6/833
Appears in Collections:Medicine publications

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