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Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets
EF Plow, MD Pierschbacher, E Ruoslahti, G Marguerie and MH Ginsberg
Human fibrinogen has an Arg-Gly-Asp-Ser (RGDS) sequence at residues 572-
575 of its A alpha-chain. Although RGDS-containing peptides inhibit
fibrinogen binding to stimulated platelets, these peptides also inhibit
platelet binding of human fibrinogen fragment X and rat fibrinogen, which
lack RGDS sequences corresponding to A alpha 572-575. Thus competition
between free RGD-containing peptides and internal RGDS sequence at A alpha
572-575 is not the basis for their inhibition of fibrinogen binding to
platelets. Addition of a Thr to the carboxy- terminus and an Asn to the
amino-terminus of the RGDS sequence, the amino acids corresponding to A
alpha 576 and 571 respectively, reduced the inhibitory potency of
RGDS-containing peptides by fourfold to tenfold. Arg-Gly-Asp-Phe (RGDF)
corresponds to A alpha 95-98, and the RGDF peptide was an effective
inhibitor of fibrinogen binding, fourfold to fivefold more potent than
RGDS. Thus, local primary structure may play an important role in
regulating the capacity of RGD sequences in proteins to interact with
specific adhesion receptors.
Volume 70,
Issue 1,
pp. 110-115,
07/01/1987
Copyright © 1987 by The American Society of Hematology
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