TAILIEUCHUNG - Báo cáo khoa học: Probing plasma clearance of the thrombin–antithrombin complex with a monoclonal antibody against the putative serpin–enzyme complex receptor-binding site

A high-affinity monoclonal antibody (M27), raised against the human thrombin–antithrombin complex, has been identifiedand characterized. The epitope recognizedbyM27 was located to the linear sequence FIREVP (residues 411– 416), located in the C-terminal cleavage peptide of regionoverlaps, by two residues, theputative binding site of antithrombin for the serpin–enzyme complex receptor. Studies in rats and with HepG2 cells in culture indicated that the Fab fragment of M27 does not block binding anduptake of the thrombin–antithrombin complex, suggesting that this region does not play a major role in the recognition and clearance of the thrombin–antithrombin complex | Eur. J. Biochem. 270 4059-4069 2003 FEBS 2003 doi Probing plasma clearance of the thrombin-antithrombin complex with a monoclonal antibody against the putative serpin-enzyme complex receptor-binding site George L. Long1 I Margareta Kjellberg2 Bruno O. Villoutreix3 and Johan Stenflo2 1 Department of Biochemistry University of Vermont Burlington VT USA department of Clinical Chemistry Lund University University Hospital Malmo Malmo Sweden 3INSERM U428 Univesstty of Paiis V Frnnce A high-affinity monoclonal antibody M27 raised against the human thrombin-antithrombin complex has been identified and characterized. The epitope recognized by M27 was located to the linear sequence FIREVP residues 411416 located in the C-terminal cleavage peptide of antithrombin. This region overlaps by two residues the putative binding site of antithrombin for the serpin-enzyme complex receptor. Studies in rats and with HepG2 cells in culture indicated that the Fab fragment of M27 does not block binding and uptake of the thrombin-antithrombin complex suggesting that this region does not play a major role in the recognition and clearance of the thrombin-antithrombin complex. M27 blocked the ability of antithrombin to inhibit thrombin as well as antithrombin cleavage both in the presence and absence of heparin. Keywords antithrombin thrombin thrombin-antithrombin complex monoclonal antibody serpin-enzyme complex receptor. Antithrombin AT a member of the serine protease inhibitor family serpin is a 58-kDa molecular mass glycoprotein that circulates in human plasma at a concentration of w 5 M 1-5 . AT modulates blood coagulation by inhibiting thrombin active factor X factor Xa and active factor IX factor IXa and thereby prevents inappropriate clot formation and thrombosis. The rate of AT-mediated inhibition of thrombin and factor Xa is increased several thousand-fold by binding of the sulfated polysaccharide heparin or heparin-like molecules. Individuals with .

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