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The goal of the present study was to determine whether platelet
glycoprotein (GP) V interacts directly with the von Willebrand factor
receptor GP Ib-IX and, if so, whether it affects the expression and
function of this receptor. A melanoma cell line that does not contain
actin-binding protein was transfected with the cDNAs coding for GP V
and for each of the three subunits of GP Ib-IX. GP V
co-immunoprecipitated and co-localized with GP Ib-IX. Although GP V
could be expressed in the absence of GP Ib-IX, the amount incorporated
in the membrane was markedly increased when GP Ib-IX was present.
Similarly, there was an enhanced expression of GP Ib-IX on the cell
surface in the presence of GP V. The binding affinity of
botrocetin-induced von Willebrand factor to GP Ib-IX was unaffected by
the presence or absence of GP V. However, the binding capacity was
increased by the presence of GP V. We conclude that GP V interacts
directly with GP Ib-IX, that GP V must associate with GP Ib-IX to be
efficiently expressed in the membrane, and that GP V increases the
binding capacity of the cells for von Willebrand factor by enhancing
the surface expression of the GP Ib-IX complex.
Volume 270,
Number 24,
Issue of June 16, pp. 14693-14699, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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