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Platelet glycoprotein IIb/IIIa complex in cultured cells. Localization in
focal adhesion sites in spreading HEL cells
J Ylanne, M Hormia, M Jarvinen, T Vartio and I Virtanen
Department of Anatomy, University of Helsinki, Finland.
A panel of mouse monoclonal antibodies (MoAbs) was raised that react with
platelet glycoproteins (GP) IIb or IIIa. On immunofluorescence, the MoAbs
reacted with 30% to 40% of the human erythroleukemia (HEL) cells. When the
HEL cells were induced to spread on fibronectin in the presence of
12-O-tetradecanoylphorbol-13-acetate (TPA), the MoAbs reacted with the
focal adhesion sites. Only some of the GPIIIa MoAbs reacted with cells
other than platelets, megakaryocytes, or HEL cells, and these showed focal
adhesion sites in cultured human endothelial cells, fibroblasts, and
epithelial cells from normal kidney tubules. They did not react, however,
with transformed fibroblasts, fibrosarcoma cells, cultured cells from
hypernephromas, or cultured human amnion epithelial cells. The results
suggest that the platelet-type GPIIb/IIIa complex is only expressed in
cells showing an ability to define megakaryoblastic differentiation.
Localization of the GPIIb/IIIa complex at the induced focal adhesion sites
in HEL cells and localization of the GPIIIa-like molecules in other cells
suggest their direct role in the adhesion process and in the actomyocin
organization of adherent cells.
Volume 72,
Issue 5,
pp. 1478-1486,
11/01/1988
Copyright © 1988 by The American Society of Hematology

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