Oxidative Modification of Fibrinogen Affects Its Binding Activity to Glycoprotein (GP) IIb/IIIa

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dc.authoridEkşioğlu-Demiralp, Emel/0000-0002-7695-0614
dc.authorwosidEkşioğlu-Demiralp, Emel/U-5708-2019
dc.contributor.authorTetik, Sermin
dc.contributor.authorKaya, Kurtulus
dc.contributor.authorDemir, M.
dc.contributor.authorEksioglu-Demiralp, Emel
dc.contributor.authorYardimci, Turay
dc.date.accessioned2024-06-12T11:11:53Z
dc.date.available2024-06-12T11:11:53Z
dc.date.issued2010
dc.departmentTrakya Üniversitesien_US
dc.description.abstractAim: Proteins are sensitive biomarkers Of human diease condition associated with oxidative stress. Alteration of protein structures by oxidants may result ill partial or complete loss of protein functions. We have investigated the effect of structural modifications induced by metal ion catalyzed oxidation of Fibrinogen oil its binding capacity to glycoprotein IIb/IIIa (GpIIb/IIIa) and human platelets. Methods: We identified and quantified of binding capacity of native and oxidized fibrinogen to its receptor in vitro by flow cytometer. Dityrosine formation oil oxidized Fibrinogen were detected spectrophotometrically. Elevated degradation products Of fibrinogen after oxidation were revealed in the HPLC analysis. The native and oxidized fibrinogen were analyzed oil mass spectrum upon digestion with tyripsin. Results: Oxidatively modified fibrinogen showed less binding activity than native fibrinogen to GpIIb/IIIa coated micro beads and human platelets whereas slightly higher binding capaticity to ADP induced Stimulated platelets. Formation of dityrosines in the amino acid side chains of fibrinogen were observed Upon Oxidation. Decreased binding capacity of oxidized fibrinogen correlated with intensities of dityrosine formation. Oxidized fibrinogen had more ion-mass intensities at higher than native fibrinogen. Clinical implications: important point is decreased of binding capacity of the oxidized fibrinogen to own receptor. The decreased rate of binding, leading to effect in the diseases of clot formation May account for the association between oxidation of fibrinogen and the incidence of effect in human diseases.en_US
dc.description.sponsorshipMarmara University [SAG/YYT-310807-0171, SAG/YLS-290506-0064]en_US
dc.description.sponsorshipThis work was is supported by Marmara University Research Grant SAG/YYT-310807-0171 and SAG/YLS-290506-0064en_US
dc.identifier.doi10.1177/1076029609339749
dc.identifier.endpage59en_US
dc.identifier.issn1076-0296
dc.identifier.issn1938-2723
dc.identifier.issue1en_US
dc.identifier.pmid19903699en_US
dc.identifier.scopus2-s2.0-76049101322en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage51en_US
dc.identifier.urihttps://doi.org/10.1177/1076029609339749
dc.identifier.urihttps://hdl.handle.net/20.500.14551/22970
dc.identifier.volume16en_US
dc.identifier.wosWOS:000274087000007en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherSage Publications Incen_US
dc.relation.ispartofClinical And Applied Thrombosis-Hemostasisen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectOxidant Stressen_US
dc.subjectFibrinogenen_US
dc.subjectGpiib/Iiiaen_US
dc.subjectFlow Cytometryen_US
dc.subjectHPLC- Mass Spectrumen_US
dc.subjectPlatelet-Aggregationen_US
dc.subjectProteinsen_US
dc.titleOxidative Modification of Fibrinogen Affects Its Binding Activity to Glycoprotein (GP) IIb/IIIaen_US
dc.typeArticleen_US

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