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Aggregation of mammalian cells expressing the platelet glycoprotein (GP)
Ib-IX complex and the requirement for tyrosine sulfation of GP Ib alpha
JF Dong, W Hyun and JA Lopez
Gladstone Institute of Cardiovascular Disease, San Francisco, CA, USA.
The glycoprotein (GP) Ib-IX complex mediates platelet aggregation in
response to high shear forces by binding von Willebrand factor (vWF) in the
plasma. We investigated the possibility that the complex could mediate a
similar phenomenon if expressed in nonhematopoietic cells. When agitated on
a tabletop shaker, CHO and L cells expressing the full complex formed large
aggregates in the presence of vWF and the modulator ristocetin. When the
rate of agitation was increased, aggregation occurred without added
ristocetin and appeared to require only the application of a physical
force. The aggregation was homophilic and temperature-dependent and
required a functional ligand- binding subunit of the GP Ib-IX complex, GP
Ib alpha. Posttranslational tyrosine sulfation of GP Ib alpha was required
for aggregate formation and stability. Thus, aggregation of cells
expressing the GP Ib-IX complex is a unique example of a ligand-receptor
interaction induced by mechanical forces and demonstrates an important
biological role for sulfation of tyrosine residues.
Volume 86,
Issue 11,
pp. 4175-4183,
12/01/1995
Copyright © 1995 by The American Society of Hematology
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