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J. Biol. Chem., Vol. 266, Issue 22, 14202-14207, 08, 1991
A Andrieux, MJ Rabiet, A Chapel, E Concord and G Marguerie
The Arg-Gly-Asp (RGD)-binding domain of GPIIb-IIIa has been localized in a
fragment of the GPIIIa subunit that includes the sequence between amino
acids 109 and 171. To examine, in a platelet membrane environment, the
activated versus nonactivated status of this domain, we have produced a
monoclonal antibody against a synthetic peptide (residues 109-128) located
within the RGD-binding region on GPIIIa. This kappa-IgM, named AC7, was
specific for GPIIIa peptide 109-128 and interacted only with activated
platelets. Fibrinogen, RGDF peptide, and the fibrinogen phi chain
decapeptide LGGAKQAGDV inhibited the binding of AC7 to ADP-stimulated
platelets. AC7 IgM and "small fragments" inhibited fibrinogen binding and
platelet aggregation in a dose- dependent fashion. Induction of AC7 binding
by D33C, a monoclonal antibody recognizing the GPIIb 426-437 sequence and
stimulating fibrinogen binding, indicated that the GPIIb 426-437 and the
GPIIIa 109- 128 sequences were both involved in a stimulation-dependent
conformational modification of the receptor. AC7 was able to recognize beta
subunits other than GPIIIa on leucocyte surfaces but only after cell
fixation with glutaraldehyde. The results are consistent with the
implication of the RGD-binding domain in receptor ligand interaction on the
platelet surface and its conformational modification and exposure upon
receptor induction.
A highly conserved sequence of the Arg-Gly-Asp-binding domain of the integrin beta 3 subunit is sensitive to stimulation
Institut National de la Sante et de la Recherche Medicale U217, Departement de Biologie, Moleculaire et Structurale, Grenoble, France.
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