Összesen 2 találat.


001-es BibID:BIBFORM095056
Első szerző:Szabó Gábor (PhD-hallgató)
Cím:Laboratory Approaches to Test the Function of Antiphospholipid Antibodies / Gábor Szabó, Péter Antal-Szalmás, Adrienne Kerényi, Krisztina Pénzes, Bálint Bécsi, János Kappelmayer
Megjegyzések:Antiphospholipid syndrome (APS) is a systemic autoimmune disorder caused by the presence of aPLs (antiphospholipid antibodies, i.e., anti-?2-glycoprotein I and anticardiolipin). Everyday practice in terms of laboratory diagnostics of APS includes determination of aPLs and well-known functional assays assessing for lupus anticoagulant (LA), in turn using various tests. According to recent guidelines, the recommended method for LA identification or exclusion is based on the Russell Viper Venom test and a sensitive activated partial thromboplastin time assay. Despite the fact that LA can be quantified in laboratory practice in this way, LA is still used as a binary parameter that is just one of the risk factors of thrombosis in APS. As of today, there are no other functional assays to routinely assess the risk of thrombosis in APS. It is well-known that APS patients display a wide range of clinical outcomes although they may express very similar laboratory findings. One way to solve this dilemma, could be if antibodies could be further delineated using more advanced functional tests. Therefore, we review the diagnostic approaches to test the function of aPLs. We further discuss how thrombin generation assays, and rotational thromboelastometry tests can be influenced by LA, and how experimental methods, such as flow cytometric platelet activation, surface plasmon resonance, or nano differential scanning fluorimetry can bring us closer to the puzzling interaction of aPLs with platelets as well as with their soluble protein ligand. These novel approaches may eventually enable better characterization of aPL, and also provide a better linkage to APS pathophysiology.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
antiphospholipid antibodies
Megjelenés:Seminars In Thrombosis And Hemostasis. - 48 : 2 (2022), p. 132-144. -
További szerzők:Antal-Szalmás Péter (1968-) (laboratóriumi szakorvos) Kerényi Adrienne (1970-) (laboratóriumi szakorvos) Pénzes-Daku Krisztina (1978-) (biológus) Bécsi Bálint (1981-) (vegyészmérnök) Kappelmayer János (1960-) (laboratóriumi szakorvos)
Internet cím:DOI
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001-es BibID:BIBFORM088736
035-os BibID:(cikkazonosító)112877
Első szerző:Szabó Gábor (PhD-hallgató)
Cím:Distinct and overlapping effects of [beta]2-glycoprotein I conformational variants in ligand interactions and functional assays / Szabó Gábor, Pénzes Krisztina, Torner Bernadett, Fagyas Miklós, Tarr Tünde, Soltész Pál, Kis Gréta, Antal Miklós, Kappelmayer János
Megjegyzések:One of the most abundant coagulation proteins is ?2-glycoprotein I (?2GPI) that is present in humans at a concentration of around 200 mg/L. Its physiological role is only partially understood, but it adopts several different structural forms the majority of which are the open and closed forms. We isolated native (circular) ?2GPI and converted it into an open conformation. The effectiveness of these procedures was assessed by Western blot and negative-staining electron microscopy. We found that in coagulation assays the open form of ?2GPI had a significant prolonging effect on fibrin formation in a dilute prothrombin time test (p < 0.001). In the dilute activated partial thromboplastin time test, both conformations had a significant prolonging effect (p < 0.001) but the open conformation was more effective. In a fluorescent thrombin generation assay both conformations slightly delayed thrombin generation with no significant effect on the quantity of formed thrombin. By using surface plasmon resonance assays, the equilibrium dissociation constants of both the open and closed conformations of ?2GPI showed a similar and strong affinity to isolated anti-?2GPI autoantibodies (Kd closed ?2GPI = 5.17 ? 10-8 M, Kd open ?2GPI = 5.56 ? 10-8 M) and the open form had one order of magnitude stronger affinity to heparin (Kd = 0.30 ? 10-6 M) compared to the closed conformation (Kd = 3.50 ? 10-6 M). The two different forms of ?2GPI have distinct effects in functional tests and in ligand binding, which may considerably affect the intravascular events related to this abundant plasma protein in health and disease.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Anti-[beta](2)-glycoprotein I
Surface plasmon resonance
Thrombin generation
[beta](2)-glycoprotein I conformations
Megjelenés:Journal of Immunological Methods. - 487 (2020), p. 112877. -
További szerzők:Pénzes-Daku Krisztina (1978-) (biológus) Torner Bernadett Fagyas Miklós (1984-) (orvos) Tarr Tünde (1976-) (belgyógyász, allergológus és klinikai immunológus) Soltész Pál (1961-) (belgyógyász, kardiológus) Kis Gréta (1979-) (molekuláris biológus) Antal Miklós (1951-) (orvos, anatómus) Kappelmayer János (1960-) (laboratóriumi szakorvos)
Pályázati támogatás:OTKA K16 120725
Internet cím:Szerző által megadott URL
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