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ISRN Cell Biology
Volume 2012 (2012), Article ID 632867, 11 pages
The Modification of Xa-ATIII-Heparin Dynamics by Protamine Sulfate
1Departments of Biological Sciences and Chemistry, Bowling Green State University, Bowling Green, OH 43403, USA
2Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403, USA
Received 27 September 2011; Accepted 10 November 2011
Academic Editor: N. Zambrano
Copyright © 2012 Martin H. Coggin and Arthur S. Brecher. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- T. Mertons, T. Nakajima, Y. Hayashi, and M. Kuro, “Hemostatic effects of low dose protamine following pulmondary bypass,” American Journal of Hematology, vol. 185, pp. 647–658, 1980.
- K. Kurachi, K. Fujikawa, G. Schmer, and E. W. Davie, “Inhibition of bovine factor IXa and factor Xaβ by antithrombin III,” Biochemistry, vol. 15, no. 2, pp. 373–377, 1976.
- J. Jesty, “Dissociation of complexes and their derivatives formed during inhibition of bovine thrombin and activated factor X by antithrombin III,” Journal of Biological Chemistry, vol. 254, no. 4, pp. 1044–1049, 1979.
- R. D. Rosenberg, “Chemistry of the hemostatic mechanism and its relationship to the action of heparin,” Federation Proceedings, vol. 36, no. 1, pp. 10–18, 1977.
- I. Bjork, C. M. Jackson, and H. Jornvall, “The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin,” Journal of Biological Chemistry, vol. 257, no. 5, pp. 2406–2411, 1982.
- I. Bjork and W. W. Fish, “Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin,” Journal of Biological Chemistry, vol. 257, no. 16, pp. 9487–9493, 1982.
- P. A. Craig, S. T. Olson, and J. D. Shore, “Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Characterization of assembly, product formation, and heparin dissociation steps in the factor Xa reaction,” Journal of Biological Chemistry, vol. 264, no. 10, pp. 5452–5461, 1989.
- A. R. Rezaie, “Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism: Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa,” Journal of Biological Chemistry, vol. 273, no. 27, pp. 16824–16827, 1998.
- A. R. Rezaie, “Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding,” Journal of Biological Chemistry, vol. 275, no. 5, pp. 3320–3327, 2000.
- A. R. Rezaie and S. T. Olson, “Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies,” Biochemistry, vol. 39, no. 39, pp. 12083–12090, 2000.
- J. A. Marcum and R. D. Rosenberg, “Anticoagulantly active heparin-like molecules from vascular tissue,” Biochemistry, vol. 23, no. 8, pp. 1730–1737, 1984.
- A. Perkash, “A comparison of the quantitative action of protamine and heparin on blood coagulation. Significance in clinical and laboratory usage,” American Journal of Clinical Pathology, vol. 73, no. 5, pp. 676–681, 1980.
- T. Sugiyama, M. Itoh, M. Ohtawa, and T. Natsuga, “Study on neutralization of low molecular weight heparin (LHG) by protamine sulfate and its neutralization characteristics,” Thrombosis Research, vol. 68, no. 2, pp. 119–129, 1992.
- M. Kontani, A. Amano, T. Nakamura, I. Nakagawa, S. Kawabata, and S. Hamada, “Inhibitory effects of protamines on proteolytic and adhesive activities of Porphyromonas gingivalis,” Infection and Immunity, vol. 67, no. 9, pp. 4917–4920, 1999.
- T. Kitani, S. C. Nagarajan, and J. N. Shanberge, “Effect of protamine on heparin-antithrombin III complexes. In vitro studies,” Thrombosis Research, vol. 17, no. 3-4, pp. 367–374, 1980.
- D. P. Thomas, T. W. Barrowcliffe, and R. E. Merton, “In vivo release of anti-Xa clotting activity by a heparin analogue,” Thrombosis Research, vol. 17, no. 6, pp. 831–840, 1980.
- M. Wolzt, A. Weltermann, M. Nieszpaur-Los et al., “Studies on the neutralizing effects of protamine on unfractionated and low molecular weight heparin (Fragmin®) at the site of activation of the coagulation system in man,” Thrombosis and Haemostasis, vol. 73, no. 3, pp. 439–443, 1995.
- Y. Okajima, S. Kanayama, and Y. Maeda, “Studies on the neutralizing mechanism of antithrombin activity of heparin by protamine,” Thrombosis Research, vol. 24, no. 1-2, pp. 21–29, 1981.
- T. Miyashita, T. Nakajima, Y. Hayashi, and M. Kuro, “Hemostatic effects of low-dose protamine following cardiopulmonary bypass,” American Journal of Hematology, vol. 64, no. 2, pp. 112–115, 2000.
- P. W. Majerus, G. H. Broze Jr., J. P. Miletick, and D. M. Tollefsen, “Anticoagulant, thrombolytic, and antiplatelet drugs,” in The Pharmacological Basis of Therapeutics, A. Goodman, T. W. Gilman, A. S. Nies, and P. Taylor, Eds., pp. 1311–1331, Pergamon Press, New York, NY, USA, 8th edition, 1990.
- A. S. Brecher, K. Hellman, and M. H. Basista, “Coagulation protein function VI: augmentation of anticoagulant function by acetaldehyde-treated heparin.,” Digestive Diseases and Sciences, vol. 44, no. 7, pp. 1349–1355, 1999.
- M. H. Coggin, R. Ahl, A. Roland, D. Beck, and A. S. Brecher, “Protamine sulfate stimulates degradation of factor Xa and the factor Xa-antithrombin complex,” Blood Coagulation and Fibrinolysis, vol. 22, no. 4, pp. 247–253, 2011.
- U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970.
- S. T. Olson and J. D. Shore, “Binding of high affinity heparin to antithrombin III. Characterization of the protein fluorescence enhancement,” Journal of Biological Chemistry, vol. 256, no. 21, pp. 11065–11072, 1981.
- S. T. Olson and J. D. Shore, “Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. The reaction step limiting heparin turnover in thrombin neutralization,” Journal of Biological Chemistry, vol. 261, no. 28, pp. 13151–13159, 1986.
- S. T. Olson, K. R. Srinivasan, I. Bjork, and J. D. Shore, “Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction,” Journal of Biological Chemistry, vol. 256, no. 21, pp. 11073–11079, 1981.
- A. R. Rezaie, “Heparin-binding exosite of factor Xa,” Trends in Cardiovascular Medicine, vol. 10, no. 8, pp. 333–338, 2000.
- S. T. Olson, I. Bjork, R. Sheffer, P. A. Craig, J. D. Shore, and J. Choay, “Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement,” Journal of Biological Chemistry, vol. 267, no. 18, pp. 12528–12538, 1992.
- U. Lindahl, G. Backstrom, L. Thunberg, and I. G. Leder, “Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 77, no. 11 I, pp. 6551–6555, 1980.
- G. A. Silverman, P. I. Bird, R. W. Carrell et al., “The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature,” Journal of Biological Chemistry, vol. 276, no. 36, pp. 33293–33296, 2001.
- J. Jesty, A. K. Spencer, and Y. Nemerson, “The mechanism of activation of factor X. Kinetic control of alternative pathways leading to the formation of activated factor X,” Journal of Biological Chemistry, vol. 249, no. 17, pp. 5614–5622, 1974.