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Relevant bibliographies by topics / Thrombin inhibitor

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Academic literature on the topic 'Thrombin inhibitor'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Thrombin inhibitor"

1

Pahl, M. V., N. D. Vaziri, F. Oveisi, J. Wang, and Y. Ding. "Antithrombin III inhibits mesangial cell proliferation." Journal of the American Society of Nephrology 7, no. 10 (1996): 2249–53. http://dx.doi.org/10.1681/asn.v7102249.

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Thrombin stimulates and heparin and heparan sulfate inhibit mesangial cell proliferation. In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation. The anticoagulant action of heparin is mediated by antithrombin III. This study investigated whether heparin's antiproliferative action is also mediated by antithrombin III. To this end, the effect of antithrombin III on thrombin-stimulated mesangial cell growth was examined. As expected, thrombin stimulated DNA synthesis and cell growth in cultured human mesangial cells. The effect of thrombin on DNA synt

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Glusa, Erika, Ellen Bretschneider, Joachim Daum, and Christiane Noeske-Jungblut. "Inhibition of Thrombin-mediated Cellular Effects by Triabin, a Highly Potent Anion-binding Exosite Thrombin Inhibitor." Thrombosis and Haemostasis 77, no. 06 (1997): 1196–200. http://dx.doi.org/10.1055/s-0038-1656137.

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SummaryTriabin, a 17 kDa protein from the saliva of the assassin bug Triatoma pallidipennis is a potent thrombin inhibitor interfering with the anion-binding exosite of the enzyme. The recombinant protein, produced by the baculovirus/insect cell system, was used to study the inhibitory effect on thrombin-mediated cellular responses. The thrombin (1 nM)-stimulated aggregation of washed human platelets and the rise in cytoplasmic calcium in platelets were inhibited by triabin at nanomolar concentrations. In contrast, the rise in calcium induced by the thrombin receptor-activating peptide (10 μM)

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Bagdy, Dániel, Gabriella Szabó, Éva Barabás, and Sándor Bajusz. "Inhibition by D-MePhe-Pro-Arg-H (GYKI-14766) of Thrombus Growth in Experimental Models of Thrombosis." Thrombosis and Haemostasis 68, no. 02 (1992): 125–29. http://dx.doi.org/10.1055/s-0038-1656336.

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SummaryThe antithrombotic action of the highly effective synthetic thrombin inhibitor D-MePhe-Pro-Arg-H (GYKI-14766) was studied in various models of experimental thrombosis. The compound administered to rats and rabbits by i. v. bolus injections, continuous i. v. infusions, subcutaneously and orally, respectively, induced significant decrease in thrombus weight (i) in a quantitative venous thrombosis model with stasis based on vascular lesion in rats, (ii) in an extracorporeal arterio-venous shunt model in rabbits, and (iii) prevented the occlusion of the vessel in arterial thrombosis induced

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Wang, Wei-Ya, Chien-Kei Wei, Che-Ming Teng, and Chin-Chung Wu. "Combined blockade of thrombin anion binding exosite-1 and PAR4 produces synergistic antiplatelet effect in human platelets." Thrombosis and Haemostasis 105, no. 01 (2011): 88–95. http://dx.doi.org/10.1160/th10-05-0305.

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SummaryThrombin exosite-1 mediates the specific binding of thrombin with fibrinogen and protease-activated receptor (PAR) 1. Exosite-1 inhibitors have been shown to effectively decrease the clotting activity of thrombin, while their antiplatelet effects are relatively weak. In the present study, the inhibitory effects of two exosite-1 inhibitors, hirugen and HD1, but not the exosite-2 inhibitor HD22, on thrombin-induced platelet aggregation and P-selectin expression were dramatically enhanced by a PAR4 antagonist, YD-3. In contrast, the PAR1 antagonist SCH-79797 did not affect the antiplatelet

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Lunven, Catherine, Christiane Gauffeny, Catherine Lecoffre, Donogh P. O’Brien, Nigel O. Roome, and Christopher N. Berry. "Inhibition by Argatroban, a Specific Thrombin Inhibitor, of Platelet Activation by Fibrin Clot-associated Thrombin." Thrombosis and Haemostasis 75, no. 01 (1996): 154–69. http://dx.doi.org/10.1055/s-0038-1650236.

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SummaryClot-associated thrombin retains amidolytic activity, and is resistant to inhibition by heparin, but not to low molecular weight thrombin inhibitors. We show that clot-associated thrombin induces platelet aggregation, is resistant to heparin:antithrombin III, less so to recombinant hirudin (rHV2Lys47) but not to argatroban, an active-site directed thrombin inhibitor. Fibrin clots prepared with human fibrinogen and thrombin were used to aggregate rabbit washed platelets assessed by single platelet counting, thromboxane B2 (TXB2) immunoassay and scanning electron microscopy. Fibrin clots

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Kaminski, M., and J. McDonagh. "Inhibited thrombins. Interactions with fibrinogen and fibrin." Biochemical Journal 242, no. 3 (1987): 881–87. http://dx.doi.org/10.1042/bj2420881.

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Fibrin-monomer-Sepharose was used to study thrombin binding to fibrin and the role of the enzyme active centre in this interaction. Binding properties of preformed enzyme-inhibitor complexes, as well as inhibition of thrombin already adsorbed to fibrin monomer, were investigated. No apparent difference was found in binding properties of phenylmethanesulphonyl fluoride-, D-Phe-Pro-Arg-CH2Cl- and dansylarginine NN-(3-ethylpentane-1,5-diyl)amide-inhibited thrombins. Also, the elution profile of phenylmethane-sulphonyl fluoride-inhibited thrombin from fibrinogen-Sepharose was identical with that o

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Finkle, Carolyn, Annie Pierre, Lorraine Leblond, Isabelle Deschenes, John DiMaio, and Peter Winocour. "BCH-2763, a Novel Potent Parenteral Thrombin Inhibitor, Is an Effective Antithrombotic Agent in Rodent Models of Arterial and Venous Thrombosis – Comparisons with Heparin, r-Hirudin, Hirulog, Inogatran and Argatroban." Thrombosis and Haemostasis 79, no. 02 (1998): 431–38. http://dx.doi.org/10.1055/s-0037-1615003.

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SummaryCurrent clinical use of heparin as an antithrombotic agent is limited by suboptimal efficacy and safety considerations. Thrombin’s central role in thrombosis makes it an attractive target to develop more effective and safer antithrombotic agents. BCH-2763 is a novel, potent (Ki: 0.11 nM), low molecular weight (1.51 kDa), bivalent direct thrombin inhibitor. The antithrombotic efficacy of BCH-2763 in vivo following i.v. bolus plus infusion in rats was compared in arterial and venous thrombosis models with two other bivalent direct thrombin inhibitors, r-hirudin and hirulog, with two catal

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Hashimoto, Masaru, Tsutomu Yamashita, Kazuhiro Oiwa, Sadahiro Watanabe, John Giddings, and Junichiro Yamamoto. "Enhancement of Endogenous Plasminogen Activator-induced Thrombolysis by Argatroban and APC and Its Control by TAFI, Measured in An Arterial Thrombolysis Model In Vivo Using Rat Mesenteric Arterioles." Thrombosis and Haemostasis 87, no. 01 (2002): 110–13. http://dx.doi.org/10.1055/s-0037-1612952.

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SummaryRecent in vitro studies have demonstrated that thrombin inhibits fibrinolysis through thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B). We have recently shown that endogenous fibrinolysis in vivo is enhanced by activated protein C (APC) and the selective thrombin inhibitor, argatroban. The aim of the present study was to examine the role of TAFI in these fibrinolytic mechanisms in vivo using purified porcine pancreatic carboxypeptidase B (PPCPB) and a specific TAFIa inhibitor, potato tuber carboxypeptidase B inhibitor (PTCI) in a newly established arteria

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Li, WX, AV Kaplan, GW Grant, JJ Toole, and LL Leung. "A novel nucleotide-based thrombin inhibitor inhibits clot-bound thrombin and reduces arterial platelet thrombus formation." Blood 83, no. 3 (1994): 677–82. http://dx.doi.org/10.1182/blood.v83.3.677.677.

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Abstract A novel thrombin inhibitor based on single-stranded (ss) deoxynucleotides with the sequence GGTTGGTGTGGTTGG (thrombin aptamer) has been recently discovered. In this study, we tested its efficacy in inhibiting clot-bound thrombin activity and platelet thrombus formation in an ex vivo whole artery angioplasty model. The thrombin aptamer showed a specific dose-dependent inhibition of thrombin-induced platelet aggregation (0.5 U/mL) in human platelet-rich plasma, with an IC50 of approximately 70 to 80 nmol/L. In an in vitro clot-bound thrombin assay system, heparin, used at clinically rel

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Li, WX, AV Kaplan, GW Grant, JJ Toole, and LL Leung. "A novel nucleotide-based thrombin inhibitor inhibits clot-bound thrombin and reduces arterial platelet thrombus formation." Blood 83, no. 3 (1994): 677–82. http://dx.doi.org/10.1182/blood.v83.3.677.bloodjournal833677.

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A novel thrombin inhibitor based on single-stranded (ss) deoxynucleotides with the sequence GGTTGGTGTGGTTGG (thrombin aptamer) has been recently discovered. In this study, we tested its efficacy in inhibiting clot-bound thrombin activity and platelet thrombus formation in an ex vivo whole artery angioplasty model. The thrombin aptamer showed a specific dose-dependent inhibition of thrombin-induced platelet aggregation (0.5 U/mL) in human platelet-rich plasma, with an IC50 of approximately 70 to 80 nmol/L. In an in vitro clot-bound thrombin assay system, heparin, used at clinically relevant con

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Dissertations / Theses on the topic "Thrombin inhibitor"

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Richardson, John Lee. "Structural and kinetic characterization of the leech derived inhibitor haemadin in complex with human [alpha]-thrombin [alpha-thrombin] structural analysis of the tsetse thrombin inhibitor in complex with bovine [alpha]-thrombin [alpha-thrombin] /." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=965976335.

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Boffa, Michael B. "Structure, function and regulation of TAFI (thrombin-activable fibrinolysis inhibitor)." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0017/NQ54402.pdf.

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Frère, Corinne. "Thrombin-Activatable Fibrinolysis Inhibitor : étude de la relation génotype-phénotype." Aix Marseille 2, 2006. http://www.theses.fr/2006AIX20695.

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Le Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) est un inhibiteur de la fibrinolyse. Les taux plasmatiques de TAFI Ag présentent une forte variabilité interindividuelle faiblement expliquée par les facteurs environnementaux. Nous avons évalué la contribution des polymorphismes du gène à la variabilité des taux de TAFI Ag. Deux polymorphismes (T+1583A et -2345 2G/1G) ont un effet additif expliquant 25 % de la variabilité des taux. Nous avons ensuite étudié le lien entre polymorphismes du gène du TAFI et risque de maladie coronaire. L’allèle Thr147 est un facteur de risque de survenue d’in

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Antovic, Jovan P. "Thrombin activatable fibrinolysis inhibitor (TAFI) in different hemorrhagic and thrombotic conditions /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-540-9/.

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Bridge, Katherine Isabella. "The role of thrombin activatable fibrinolysis inhibitor in abdominal aortic aneurysms." Thesis, University of Leeds, 2015. http://etheses.whiterose.ac.uk/10749/.

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Thrombin-activatable fibrinolysis inhibitor (TAFI) prevents the breakdown of fibrin clots through its action as an indirect inhibitor of plasmin. Patients with abdominal aortic aneurysms (AAA), in common with a number of cardiovascular diseases, display an altered fibrin clot structure, with denser clots that have smaller pores and an increased resistance to lysis. Murine studies have implicated a potential role for TAFI in AAA disease. This study aimed to investigate the role of TAFI in human AAA, and to complement this with an investigation into the effect of TAFI inhibition on AAA developme

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LIU, YIDAN. "A Novel Method for the Quantitative Evaluation of Fibrinogen Coagulation." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_theses/19.

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Fibrinogen aggregation is the last step in blood coagulation. Inhibition of fibrinogen aggregation could lead to anticoagulation effects. However, there is no good method for the ready evaluation of fibrinogen coagulation. A commonly used path method is slow and requires an expensive instrument. In this project, we have developed a microplate reader and In evaluating inhibitors of fibrinogen coagulations there is no good method. As an important process in hemostasis, fibrinogen coagulation is often detected by micro-plate reader. In our test of fibrinogen coagulation, we improved the observing

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Musashi, Kunihoro. "Thrombin inhibitor reduces leukocyte-endothelial cell interactions and vascular leakage after scatter laser photocoagulation." Kyoto University, 2007. http://hdl.handle.net/2433/135742.

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Huq, F. Y. "Changes in thrombin activatable fibrinolysis inhibitor and its role in normal pregnancy and pre-eclampsia." Thesis, University College London (University of London), 2017. http://discovery.ucl.ac.uk/1561635/.

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Yang, Zhilu, Si Zhong, Ying Yang, et al. "Polydopamine-mediated long-term elution of the direct thrombin inhibitor bivalirudin from TiO₂ nanotubes for improved vascular biocompatibility." Royal Society of Chemistry, 2014. https://tud.qucosa.de/id/qucosa%3A36252.

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Thrombosis and restenosis are two major complications associated with current commercial vascular stents. In situ regeneration of a healthy endothelium has been recognized as a promising strategy to address these issues. Numerous strategies have been explored for this goal. However, in most of the cases, they only focused on enhancing endothelial cell growth, ignoring antithrombotic requirements and the competition between smooth muscle cells (SMCs) and endothelial cells (ECs) for their growth. This resulted in non-satisfying clinical results. In this study, we created a multifunctional surfac

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Guéret, Pierre. "Développement clinique de l'EP217609 et de son antidote l'avidine." Thesis, Brest, 2017. http://www.theses.fr/2017BRES0130.

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Les pentasaccharides sont des inhibiteurs indirects du facteur Xa ayant des profils pharmacocinétiques très prédictibles. En raison de la liaison de forte affinité des pentasaccharides à l'antithrombine, cette pharmacocinétique peut être prédite mais aussi transférée à d'autres molécules qui leur sont liées de manière covalente. L'EP42675 combine dans une seule molécule, une antithrombine directe réversible peptidomimétique (analogue de l'α-NAPAP), et un pentasaccharide inhibiteur indirect du facteur Xa antithrombine dépendant (analogue du fondaparinux). L'EP217609 est le dérivé biotinylé de l

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Books on the topic "Thrombin inhibitor"

1

Claeson, Goran, Michael F. Scully, Vijay V. Kakkar, and John Deadman, eds. The Design of Synthetic Inhibitors of Thrombin. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-2418-6.

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Burger, Christina F., Melissa L. Bellomy, and Joseph J. Schlesinger. Coagulation System. Edited by Matthew D. McEvoy and Cory M. Furse. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190226459.003.0091.

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Anticoagulation is increasingly prevalent in the general population and poses a significant risk of increased bleeding in patients needing urgent or emergent surgical procedures. There are two main classes of direct or anticoagulants: direct thrombin inhibitors and factor Xa inhibitors. Management of these patients requires assessment of bleeding risk, possible reversal of anticoagulation, and subsequent management after surgery to prevent postoperative complications associated with either bleeding or clot formation (due to cessation of anticoagulants). This chapter covers the proper assessmen

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The Design of synthetic inhibitors of thrombin. Plenum Press, 1993.

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Scully, Michael F., Goran Claeson, Vijay V. Kakkar, and John Deadman. The Design of Synthetic Inhibitors of Thrombin. Springer, 2013.

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Struzebecher. Recent Developments in the Field of Thrombin Inhibitors: A special issue of the journal Enzyme Inhibition. Routledge, 1995.

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Buchanan, Michael R., Ph. D., Brister Stephanie J, and Ofosu Frederick A, eds. Thrombin: Its key role in thrombogenesis : implications for its inhibition clinically. CRC Press, 1995.

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(Editor), Goran Claeson, Michael F. Scully (Editor), Vijay V. Kakkar (Editor), and John Deadman (Editor), eds. The Design of Synthetic Inhibitors of Thrombin (Advances in Experimental Medicine and Biology). Springer, 1994.

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Capodanno, Davide. Bivalirudin and argatroban. Edited by Raffaele DeCaterina. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0052.

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The central role of thrombin in the process of clot formation makes it an important therapeutic target. Heparin is a potent anticoagulant, but has a number of limitations, in that—for example—it does not bind clot-bound thrombin, activates platelets, and may determine heparin-induced thrombocytopenia (HIT). Bivalirudin and argatroban, which belong to the class of intravenous direct thrombin inhibitors, overcome many of the limitations of heparin. Bivalirudin is currently indicated for patients undergoing percutaneous coronary intervention, patients with non-ST-segment elevation acute coronary

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Ofosu, Frederick A., Stephanie J. Brister, and Michael R. Buchanan. ThrombinIts Key Role in Thrombogenesis-Implications for Its Inhibition. CRC, 1994.

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(Editor), H. K. Breddin, and J. M. Walenga (Editor), eds. Clinical Management of Thrombotic and Cardiovascular Disorders With Thrombin Inhibitors, the Role of Argatroban: The Role of Argatroban (Pathophysiology of Haemostasis and Thrombosis). Not Avail, 2003.

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Book chapters on the topic "Thrombin inhibitor"

1

Zingali, Russolina B., and Ana Cristina Ferraz Nogueira. "Bothrojaracin – A Potent Thrombin Inhibitor." In Toxins and Hemostasis. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9295-3_12.

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Raj, Satish R., S. R. Wayne Chen, Robert S. Sheldon, et al. "Thrombin Activatable Fibrinolytic Inhibitor and Venous Thrombosis." In Encyclopedia of Molecular Mechanisms of Disease. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_1736.

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Banner, David W., and Paul Hadváry. "Inhibitor Binding to Thrombin: X-Ray Crystallographic Studies." In Advances in Experimental Medicine and Biology. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-2418-6_3.

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Shuman, Robert T., Robert B. Rothenberger, Charles S. Campbell, et al. "Prevention of reocclusion by a thrombin inhibitor (LY282056)." In Peptides. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_322.

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Scholz, U., A. Siegemund, T. Siegemund, S. Petros, and L. Engelmann. "Endogenous Thrombin Potential and Thrombin Activatable Fibrinolysis Inhibitor in Patients with Hemophilia and von-Willebrand disease." In 33rd Hemophilia Symposium. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18260-0_40.

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Ghosh, Arun K., and Sandra Gemma. "Development of Direct Thrombin Inhibitor, Dabigatran Etexilate, as an Anticoagulant Drug." In Structure-Based Design of Drugs and Other Bioactive Molecules. Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527665211.ch15.

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Szewczuk, Zbigniew, Bernard F. Gibbs, Shi-Yi Yue, and Yasuo Konishi. "A new cyclic thrombin exo-site inhibitor with improved potency and proteolytic stability." In Peptides 1992. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_249.

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Powers, James C., and Chih-Min Kam. "Synthetic Substrates and Inhibitors of Thrombin." In Thrombin. Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3296-5_4.

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Maraganore, John M. "Pre-Clinical and Clinical Studies on Hirulog: A Potent and Specific Direct Thrombin Inhibitor." In Advances in Experimental Medicine and Biology. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-2418-6_20.

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Wakselman, M., J. P. Mazaleyrat, R. C. Lin, et al. "Design, synthesis and study of a selective cyclopeptidic mechanism-based inhibitor of human thrombin." In Peptides. Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_213.

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Conference papers on the topic "Thrombin inhibitor"

1

Saeki, T., K. HARADA, T. Youshimura, et al. "MODE OF ACTION OF A NOVEL ANTI-PLATELET AGENT (E-5510)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643427.

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A novel anti-platelet agent, 4-cyano-5,5-bis(4-methoxy-phenyl)-4-pentenoic acid(E-5510), has been shown to inhibit platelet aggregation and secretion induced by thrombin as well as by other inducers such as ADP, collagen and PAF. Although E-5510 can act as a cyclooxygenase inhibitor,inhibition of cyclooxygenase may not be the primary mode of action since this compound effectively inhibits thrombin-induced platelet activation. In this paper, effects^of E-5510 on arachidonic acid (AA) metabolism, intracellular Ca++ and cAMP in human platelets are examined.(1) Effect on AA metabolism. Platelets p

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Puri, R. N., F. Zhou, H. Bradford, E. J. Gustafson, R. F. Colman, and R. W. Colman. "HIGH MOLECULAR WEIGHT KININOGEN SPECIFICALLY BLOCKS THROMBIN-INDUCED AGGREGATION BY INHIBITING PLATELET CALPAIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643860.

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We have previously shown that platelet-aggregation induced by alpha-thrombin (1.7 nM) involves complete cleavage of the surface membrane polypeptide, Mr = 100 kDa (MP 100) labeled by FSBA in intact platelets. The failure to cleave MP100 in membrane preparations or in platelets treated with metabolic inhibitors or leupeptin, suggested that thrombin was acting by activating platelet calpain. Since high molecular weight kininogen (HMWK) is the most potent plasma inhibitor of calpain(s), we now report that HMWK inhibited thrombin-induced aggregation in a dose-dependent manner over a range of plasm

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Liu, Hua-zhen, Wei Chen, Qi-ying Liu, Xia Zhang, Li-xiu Wang, and Cheng-wu Chi. "A NEW PEPTIDE THROMBIN INHIBITOR FROM STREPTOMYCES GRISEUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644330.

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A new peptide thrombin inhibitor was found in the Streptomyces griseus strain 254 isolated from a soil sample from Tongan, Fujian province, China, the inhibitor being a secondary metabolic product. The production of the inhibitor reached a maximum after 3 days culture of bacteria at 28°C in a rotary shaker. The inhibitor excreted in the culture filtrate was purified by absorption on macroporous resin, followed by ion exchange chromatography on DEAE-52, CM-32 cellulose, affinity chromatography on the immobilized thrombin and high performance liquid chromatography. The amino acid composition of

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Booth, N. A., A. Reith, and B. Bennett. "A PLASMINOGEN ACTIVATOR INHIBITOR (PAI-2) CIRCULATES IN TWO HIGH MOLECULAR WEIGHT FORMS IN PREGNANCY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644459.

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Normal vascular endothelium and platelet α-granules contain an inhibitor of plasminogen activator (PAI-1) of about 48000 molecular weight, which is released by stimuli such as thrombin. An immunologically distinct inhibitor (PAI-2) of about 47000 molecular weight has been purified from placenta and from a histiocytic cell line U-937. The level of PA-inhibition in plasma is raised in late pregnancy and this may be due to increases in PAI-1 or in PAI-2 or in both.Using SDS-PAGE and zymography on fibrin/plasminogen /u-PA detector gels, we have found that normal plasma contains a band of inhibitio

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Fernandez, F., B. Schmidt, M. Andrew та F. A. Ofosu. "α2-MACROGLOBULIN IS A MORE IMPORTANT INHIBITOR OF THROMBIN IN INFANT PLASMA THAN IN ADULT PLASMA". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644267.

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The concentrations of the three major inhibitors of thrombin (IIa) differ significantly in adult and infant plasma. The extent to which these differences contribute to the rates and profiles of IIa inhibition in infant and adult plasma is unknown. We determined this by adding 2 NIH U/mL of I-human α-IIa to anequal volume of defibrinated plasma for 30s at 37°C. After SDS�PAGE and autoradiography, free Ila and complexes of IIa with antithrombin III (IIa-ATIII), heparin cofactor II (IIa-HCII) and α2-macroglobulin (αa-α2M) were quantitated in 3 types of pooled plasmas: cord; 6 month old infant and

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Visser, A., and D. G. Meuleman. "IRREVERSIBLE INHIBITION OF THE THROMBIN-MEDIATED SIGNAL TRANSFER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644808.

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The inhibition of the thrombin-mediated signal transfer by a common irreversible inhibitor Z of the factor Xa complex (Xc a) and thrombin has been analysed for the two-step process of the Xc a-triggered formation of thrombin andthe consecutive splitting ok a thrombin-specific substrate S. Assuming that both proteolytic processes follow simple Michaelis—Menten kinetics, that the inhibition reactions are second-order and that the prothrombin and irreversible inhibitor are in excess it can be shown that:1. clotting time (tc) is inversely proportional to the time-averaged thrombin concentration2.

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Ofosu, F. A., G. J. Modi, M. R. Buchanan, J. Hirsh, and M. A. Blajchman. "HEPARIN IS NOT AN EFFICIENT INHIBITOR OF THE FACTOR Xa-DEPENDENT ACTIVATION OF FACTOR V AND FACTOR VIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642931.

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Abstract:

We have previously proposed that the steps in coagulation most sensitive to inhibition by heparin are the thrombin-dependent activation of factor V and factor VIII. This observation was based on the demonstration that therapeutic concentrations of heparin or 1μM of the thrombin specific inhibitor, phe-pro-arg CH2Cl (PPACK) completely inhibited the activation of prothrombin when contact-activated plasma (CAP) was recalcified for up to 1 min. Under similar conditions, heparin and PPACK only partially inhibited the activation of factor X. Moreover, the addition of thrombin (lOnM) to CAP 1 min bef

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Bagdy, D., É. Bara-bás, L. Sebestyén, et al. "CORRELATION BETWEEN THE ANTICOAGULANT AND ANTIPLATELET EFFECT OF D-PHE-PRO-ARG-H (RG-2958)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643448.

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Abstract:

Anticoagulants usually have no antiplatelet effect and platelet function inhibitors do not interact with the coagulation factors. Since thrombin has a decisive role in thrombus formation (growth and stabilization), inhibitors of the effect of thrombin on platelets may be of special importance in developing a novel type of anticoagulant with antiplatelet properties.D-Phe-Pro-Arg-H /I/ designed and synthetized in our Institute was found to be a highly specific,reversible non-competitive inhibitorgOf thrombin,a specific platelet agonist. (K.= 1x10-8 M). /I/ was administered parenterally and orall

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Ellis, V. E., M. F. Scully, and V. V. Kakkar. "KINETICS OF HEPARIN CO-FACTOR II (HCII):THROMBIN AND ANTITHROMBIN III (ATIII):THROMBIN INTERACTION. MOLECULAR WEIGHT DEPENDENCY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644350.

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Abstract:

The influence of increasing concentrations of heparin of different molecular mass (Mr) has been compared in potentiation of the rate of HCII:thrombin interaction and of ATIII:thrombin interaction under pseudo first order conditions. Unfractionated and fractionated heparin showed a concentration dependent ascending and descending limb of stimulation of the rate which was closely similar for both inhibitors. Unfractionated heparin and fractions of 16.5 KDa or less showed a peak acceleration of the rate of interaction of thrombin with both inhibitors at 0.3×10−6 heparin although the observed maxi

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Cheung, A., and K. F. Hebert. "A TUMOR SERINE PROTEASE INHIBITOR WHICH MAY FUNCTION AS A TISSUE PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644448.

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A protease inhibitor has been isolated from human colorectal adenocarcinomas by extraction with a low ionic strength-buffer and a combination of concanavalin A-Sepharose, Sephadex G-200, DEAE cellulose and chromatofocusing steps. The preparation appeared to be homogeneous upon gel exclusion chromatography and SDS polyacrylamide gel electrophoresis. It had an apparent Mr of ~66,000 and its isoelectric point was 4.6-4.7. The inhibitor was able to bind and inhibit urokinase, plasmin, trypsin, tissue plasminogen activator and thrombin. The bindings appeared to be stoichiometric and relative fast a

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