novel non-peptide fibrinogen receptor antagonist, induces conformational changes in glycoprotein lib/lila
نویسندگان
چکیده
Arg-Gly-Asp (RGD) is an amino acid sequence in fibrinogen recognized by platelet glycoprotein (GP) lIb/IlIa. Recently, it was found that RGD peptide binding to GPIIb/IIIa leads to conformational changes in the complex that are associated with the acquisition of high-affinity fibrinogen-binding function. In this study, we found that tetrafibricin, a novel non-peptidic GPIIb/IIIa antagonist, induced similar conformational changes in GPIIb/IIIa as did RGD peptides. Tetrafibricin increased the binding of purified inactive GPIIb/IIIa to immobilized pl-80, a
منابع مشابه
Platelet Glycoproteins LIb and Lila Associated With Blood Monocytes Are Derived From Platelets
Platelet glycoprotein lIb/Illa (GP lIb/Illa). the receptor complex for fibrinogen, has been regarded as a megakaryocyte/platelet lineage-restricted antigen. Recently. however. it has been reported that GP lIb/Illa is expressed in blood monocytes. Studies were performed to establish the origin and immunological characteristics of monocyteassociated glycoproteins lIb and lIla (GPs lIb and lIla). ...
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