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Effects of the cell adhesion peptide, Arg-Gly-Asp-Ser, on responses of
washed platelets from humans, rabbits, and rats
EJ Harfenist, MA Packham and JF Mustard
Department of Biochemistry, University of Toronto, Ontario, Canada.
Fibrinogen is a cofactor in the aggregation of human platelets, and is
required for ADP-induced aggregation of washed platelets; however,
exogenous fibrinogen is not required for ADP-induced aggregation of washed
platelets from rabbits or rats. Because with human platelets the cell
adhesion peptide, Arg-Gly-Asp-Ser (RGDS), inhibits aggregation and the
binding of 125I-fibrinogen to ADP-stimulated platelets, its effects on
rabbit and rat platelets were studied to investigate the differences in the
fibrinogen requirements of platelets from the three species. RGDS (50
mumol/L) caused greater than 80% inhibition of thrombin- induced or (ADP +
fibrinogen)-induced aggregation of human platelets, but only 3% to 9%
inhibition of the aggregation of rabbit or rat platelets, regardless of
whether fibrinogen was added. RGDS inhibited the binding of 125I-fibrinogen
to ADP-stimulated human platelets by 80% to 90%, but by only 15% to 27% in
the case of rabbit or rat platelets. The differences were due to the
species of platelets, since human and rabbit fibrinogens gave similar
results. In addition, RGDS failed to displace fibrinogen from the surface
of rabbit platelets that had been stimulated with ADP. Thus, there are
species differences in the ability of the cell adhesion peptide, RGDS, to
block the platelet fibrinogen receptor, even within the mammalian species.
Volume 71,
Issue 1,
pp. 132-136,
01/01/1988
Copyright © 1988 by The American Society of Hematology
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