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Blood, Vol. 93 No. 12 (June 15), 1999:
pp. 4256-4263
The Glycoprotein Ib/IX Complex Regulates Cell Proliferation
Shuju Feng,
Nicolaos Christodoulides, and
Michael H. Kroll
From the VA Medical Center, Baylor College of Medicine and Rice
University, Houston, TX.
The glycoprotein (Gp) Ib/IX complex contains three transmembranous
leucine-rich repeat polypeptides (GpIb , GpIb , and GpIX) that form
the platelet von Willebrand factor (vWF) receptor. GpIb/IX functions to
effect platelet adhesion, activation, and aggregation under conditions
of high shear stress. GpIb/IX is expressed late in the ontogeny of
megakaryocytes, the precursor cell that releases platelets when it
reaches its terminal stage of differentiation. Because signal pathways
can be reused at different stages of development by integration with
different effector pathways and because cellular adhesion through other
receptor families often modulates cell growth, the hypothesis that
GpIb/IX regulates cell growth was investigated. The surface expression
of recombinant GpIb decreases the proliferation of transduced CHO
cells. GpIb causes growth arrest in the G1 phase of the cell cycle
associated with the induction of the cyclin-dependent kinase inhibitor
p21. G1 arrest induced by recombinant GpIb in heterologous cells
requires signaling through the 14-3-3 binding domain of GpIb and
is partially dependent on its engagement by the extracellular ligand
vWF. Growth arrest induced by the expression of recombinant GpIb/IX is
followed by apoptosis of the transduced cells. The endogenous
expression of GpIb in human hematopoietic cells is associated with
decreased proliferation. These results suggest that the expression of
the GpIb/IX complex regulates megakaryocyte growth.
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