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50-kD integrin-associated protein does not detectably influence several
functions of glycoprotein IIb-IIIa complex in human platelets
T Fujimoto, K Fujimura, M Noda, T Takafuta, T Shimomura and A Kuramoto
Department of Hematology and Oncology, Hiroshima University, Japan.
A 50-kD integrin-associated protein (IAP) has been reported to be
associated with beta 3 integrins and to modulate their function, especially
vitronectin receptor in human erythroleukemia (HEL) cells and leukocyte
response integrin in neutrophils. We studied the involvement of IAP in the
function of platelet beta 3 integrin, glycoprotein (GP) IIb-IIIa complex.
IAP was a widely distributed protein and was also expressed in the cells
that do not have beta 3 integrin. Platelets from a patient with
thrombasthenia, which lack GPIIb and IIIa, expressed IAP as well as normal
platelets. Neither platelet aggregation nor intracellular Ca2+ elevation
after stimulation was influenced by the anti-IAP antibody, B6H12, which was
reported to be inhibitory for other beta 3 integrins. The expression level
of GPIIb- IIIa complex was not influenced by coexpression of human IAP in
the transfected Chinese hamster ovary (CHO) cells. IAP did not facilitate
the binding of soluble fibrinogen to the CHO cells expressing GPIIb- IIIa
complex. Furthermore, cell adhesion onto the immobilized fibrinogen via
GPIIb-IIIa complex was not inhibited by B6H12 in HEL cells and was not
altered by coexpression of human IAP in CHO cells. We concluded that
expression of IAP is regulated independently with that of GPIIb-IIIa
complex and that IAP does not influence the function of GPIIb-IIIa complex.
Volume 86,
Issue 6,
pp. 2174-2182,
09/15/1995
Copyright © 1995 by The American Society of Hematology
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