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Antithrombin

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Elliott M Antman – One of the best experts on this subject based on the ideXlab platform.

  • hirudin in acute myocardial infarction thrombolysis and thrombin inhibition in myocardial infarction timi 9b trial
    Circulation, 1996
    Co-Authors: Elliott M Antman

    Abstract:

    Background The TIMI 9 trial evaluated whether the direct Antithrombin hirudin is more effective than an indirect-acting Antithrombin, heparin, as adjunctive therapy for thrombolysis in myocardial infarction. Methods and Results Patients (n=3002) with acute myocardial infarction were treated with aspirin and either accelerated-dose tissue plasminogen activator (TPA) or streptokinase. They were randomized within 12 hours of symptoms to receive either intravenous heparin (5000 U bolus followed by infusion of 1000 U/h) or hirudin (0.1 mg/kg bolus followed by infusion of 0.1 mg/kg per hour). The infusions of both Antithrombins were titrated to a target activated partial thromboplastin time (aPTT) of 55 to 85 seconds and were administered for 96 hours. Patients randomized to hirudin were significantly more likely to have an aPTT measurement in the target range (P<.0001). The primary end point (death, recurrent nonfatal myocardial infarction, or development of severe congestive heart failure or cardiogenic shock...

Klaus T Preissner – One of the best experts on this subject based on the ideXlab platform.

  • inhibition of thrombin by Antithrombin iii and heparin cofactor ii in vivo
    Thrombosis and Haemostasis, 1995
    Co-Authors: Lori Dewar, Y Song, Myron Kulczycky, Morris A. Blajchman, Fenton Jw Nd, Maureen Andrew, Maxence Delorme, Jeffrey S. Ginsberg, Klaus T Preissner

    Abstract:

    The critical role of thrombin in the pathogenesis of venous and arterial thrombosis, and the effectiveness of glycosaminoglycans as antithrombotic drugs are well known. Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical use,r of heparin. Recent clinical and experimental studies have demonstrated that another glycosaminoglycan, dermatan sulfate, is uneffective antithrombotic drug. Dermatan sulfate catalyses the inhibition of thrombin by heparin cofactor II. The concentrations of heparin cofactor II are higher in the plasmas of individuals with congenital Antithrombin III deficiency and pregnant women than controls. The role of heparin cofactor II as a physiologic thrombin inhibitor is unknown. Enzyme-linked immunosorbent assays were used to quantify-thrombin-heparin cofactor II and thrombin-Antithrombin III endogenous to the plasmas of adult Antithrombin III-Hamilton deficient subjects, their siblings with normal Antithrombin III levels, pregnant women at term and 3 to 5 days after delivery. Both thrombin-Antithrombin III and thrombin-heparin cofactor II complexed with vitronectin were detected in all the plasmas. Significantly, the concentrations of thrombin-heparin cotactor II-vitronectin were higher in the plasmas of congenital untithrombin III deficient subjects and in preand post-delivery plasmas than those of normal subjects. In addition, the concentrations at thrombin-heparin cofactor II decreased 3 to 5 days after delivery, reflecting the disappearance of the catalytically active dermatan sultate elaborated by the placenta. Thus, heparin cofactor II normally inactivates thrombin in vivo, with its role increasing in conditions associated with high levels of heparin cofactor II and/or dermatan sultate

Johan Stenflo – One of the best experts on this subject based on the ideXlab platform.

  • probing plasma clearance of the thrombin Antithrombin complex with a monoclonal antibody against the putative serpin enzyme complex receptor binding site
    FEBS Journal, 2003
    Co-Authors: George L. Long, Margareta Kjellberg, Bruno O Villoutreix, Johan Stenflo

    Abstract:

    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 411–416), 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.