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Platelet glycoprotein IIb-IIIa (alpha IIb beta 3 integrin) confers
fibrinogen- and activation-dependent aggregation on heterologous cells
MM Frojmovic, TE O'Toole, EF Plow, JC Loftus and MH Ginsberg
Department of Physiology, McGill University, Montreal, Quebec, Canada.
To analyze molecular mechanisms of platelet aggregation, we have studied
the aggregation of Chinese hamster ovary (CHO) cells expressing between 1
and 4 x 10(5) recombinant human glycoprotein (GP) IIb-IIIa molecules per
cell (A5 cells). These cells aggregated as measured by the disappearance of
single cells during rotary agitation. Aggregation was dependent on the
presence of extracellular fibrinogen (approximately 500 nmol/L) and
divalent cations, and required prior activation of the GPIIb-IIIa. A
synthetic peptide (GRGDSP) and monoclonal anti-GPIIb-IIIa antibody (2G12)
that block platelet aggregation also blocked aggregation of these cells.
Parent CHO cells or those expressing recombinant GPIIb-IIIa containing a
point mutation that causes variant thrombasthenia both failed to aggregate
when stimulated in the presence of fibrinogen. These data show that GPIIb-
IIIa is the only unique platelet surface component required for
aggregation.
Volume 78,
Issue 2,
pp. 369-376,
07/15/1991
Copyright © 1991 by The American Society of Hematology
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