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Human platelet glycoprotein V: its role in enhancing expression of the
glycoprotein Ib receptor
DC Calverley, M Yagi, SM Stray and GJ Roth
Hematology Section, Seattle Veterans Affairs Medical Center, Seattle, WA
98108, USA.
Platelet adhesion to an injured blood vessel wall is a critical initiating
step in hemostasis mediated by a four member receptor complex (glycoprotein
Ib/V/IX) interacting with plasma von Willebrand factor (vWF). The function
of the GPV subunit within this complex is presently undefined. To study the
role of glycoprotein (GP) V within the GPIb receptor complex, we
transfected the GPV subunit gene into a hematopoietic cell line that
constitutively expresses the other three subunits (human erythroleukemia
[HEL] cells). Using flow cytometry, we found transfected GPV was surface
expressed in HEL cells; this, in turn, led to increased surface expression
of the ligand-binding GPIb alpha and GPIX subunits. Radioligand binding
assays showed that GPV- transfected HEL cells bound more vWF than their
non- or mock- transfected counterparts. We employed confocal microscopy of
GPV- transfected HEL cells to show that GPV colocalizes with GPIb alpha on
the cell surface. These findings suggest that the GPV subunit plays a role
within the GPIb receptor complex by enhancing Ib alpha surface expression.
Volume 86,
Issue 4,
pp. 1361-1367,
08/15/1995
Copyright © 1995 by The American Society of Hematology

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