1. Distinct and overlapping effects of β2-glycoprotein I conformational variants in ligand interactions and functional assays
- Author
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Krisztina Pénzes, Tünde Tarr, Gábor Szabó, János Kappelmayer, Miklós Fagyas, Miklós Antal, Bernadett Torner, Gréta Kis, and Pál Soltész
- Subjects
0301 basic medicine ,biology ,medicine.diagnostic_test ,Chemistry ,Immunology ,Heparin ,Ligand (biochemistry) ,Fibrin ,law.invention ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,Western blot ,Coagulation ,law ,biology.protein ,Biophysics ,medicine ,Immunology and Allergy ,Electron microscope ,Surface plasmon resonance ,β2 glycoprotein i ,030215 immunology ,medicine.drug - Abstract
One of the most abundant coagulation proteins is β2-glycoprotein I (β2GPI) 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) β2GPI 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 β2GPI had a significant prolonging effect on fibrin formation in a dilute prothrombin time test (p
- Published
- 2020
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