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| http://purl.uniprot.org/citations/21529934 | http://www.w3.org/2000/01/rdf-schema#comment | "Platelet adhesion to adsorbed plasma proteins, such as fibrinogen (Fg), has been conventionally thought to be mediated by the GPIIb/IIIa receptor binding to Arg-Gly-Asp (RGD)-like motifs in the adsorbed protein. In previous studies, we showed that platelet adhesion response to adsorbed Fg and Alb was strongly influenced by the degree of adsorption-induced protein unfolding and that platelet adhesion was only partially blocked by soluble RGD, with RGD-blocked platelets adhering without activation. Based on these results, we hypothesized that in addition to the RGD-specific GPIIb/IIIa receptor, which mediates both adhesion and activation, a non-RGD-specific receptor set likely also plays a role in platelet adhesion (but not activation) to both Fg and albumin (Alb). To identify and elucidate the role of these receptors, in addition to GPIIb/IIIa, we also examined the GPIb-IX-V receptor complex, which has been shown to mediate platelet adhesion (but not activation) in studies by other groups. The platelet suspension was pretreated with either a GPIIb/IIIa-antagonist drug Aggrastat(®) or monoclonal antibodies 6B4 or 24G10 against GPIb-IX-V prior to adhesion on Fg- and Alb-coated OH- and CH(3)-functionalized alkanethiol self-assembled monolayer surfaces. The results revealed that GPIIb/IIIa is the primary receptor set involved in platelet adhesion to adsorbed Fg and Alb irrespective of their degree of adsorption-induced unfolding, while the GPIb-IX-V receptor complex plays an insignificant role. Overall, these studies provide novel insights into the molecular-level mechanisms mediating platelet interactions with adsorbed plasma proteins, thereby assisting the biomaterials field develop potent strategies for inhibiting platelet-protein interactions in the design of more hemocompatible cardiovascular biomaterials and effective anti-thrombotic therapies."xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biomaterials.2011.04.011"xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/author | "Sivaraman B."xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/author | "Latour R.A."xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/name | "Biomaterials"xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/pages | "5365-5370"xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/title | "Delineating the roles of the GPIIb/IIIa and GP-Ib-IX-V platelet receptors in mediating platelet adhesion to adsorbed fibrinogen and albumin."xsd:string |
| http://purl.uniprot.org/citations/21529934 | http://purl.uniprot.org/core/volume | "32"xsd:string |
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