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Efficient surface expression of platelet GPIIb-IIIa requires both subunits
TE O'Toole, JC Loftus, EF Plow, AA Glass, JR Harper and MH Ginsberg
Committee on Vascular Biology, Research Institute of Scripps Clinic, La
Jolla, CA 92037.
Platelet membrane GPIIb-IIIa is a member of the integrin family of
heterodimeric adhesion receptors. Processing and export of certain
leukocyte and melanoma integrins is disrupted in cells lacking one subunit.
We found that surface expression of GPIIb-IIIa, measured by fluorescent
activated cell sorting or by surface labeling, required cotransfection of
both subunits. In contrast, surface expression was not detected when the
subunits were transfected individually. Immunoprecipitation of
metabolically labeled transfected cells confirmed the presence of
comparable levels of intracellular protein in all cases. When both subunits
were transfected, post-translational cleavage of Pro-GPIIb to yield GPIIb
heavy chain was also seen, while transfection with GPIIb alone resulted in
coprecipitation of Pro-GPIIb with a second band that may be an endogenous
beta subunit. Pro-GPIIb in these transfectants was not processed to yield
GPIIb heavy chain. When transfected into COS cells alone, transiently
expressed GPIIIa remained intracellular and did not appear to complex with
any endogenous proteins. Thus, surface expression of processed GPIIb-IIIa
depends on the presence of both subunits; the coordinate reduction of both
subunits observed in some cases of Glanzmann's thrombasthenia may result
from mutation affecting only one.
Volume 74,
Issue 1,
pp. 14-18,
07/01/1989
Copyright © 1989 by The American Society of Hematology
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