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SERPINC1  -  serpin peptidase inhibitor, clade C...

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Disease relevance of MGC127984

  • These data indicate that antithrombin III may play a role in the progression of HIV-1 disease [1].
  • Antithrombin III-independent effect of depolymerized holothurian glycosaminoglycan (DHG) on acute thromboembolism in mice [2].
  • Hereditary deficiency of antithrombin-III (AT-III), the major heparin cofactor in human plasma, is a well-established cause of recurrent venous thrombosis [3].
  • Our data indicate that anti-viral inactive ATIII can be activated having promising anti-viral properties as complementary candidate for the treatment of HIV infection [4].
  • Antithrombin III levels in the plasma appeared to drop during anaphylaxis but were not significantly depressed (p greater than or equal to 0.5) [5].

High impact information on MGC127984


Biological context of MGC127984


Anatomical context of MGC127984


Associations of MGC127984 with chemical compounds


Regulatory relationships of MGC127984

  • These data suggest that prothrombin fragment 2 may be an important factor in controlling the localization of clot formation by regulating the interaction between thrombin and antithrombin III [20].

Other interactions of MGC127984

  • The apparent efficiency of prothrombin activation, however, is dampened by the presence of functional antithrombin III on the vessel wall [10].
  • As predicted from the x-ray structure, des-PPW is remarkably sensitive to the bovine pancreatic trypsin inhibitor, with a K(i) over 3 x 10(3) times tighter relative to thrombin, but des-PPW is also markedly less susceptible to inactivation by antithrombin III, with a k(on) that is over 100-fold lower [21].
  • Inhibition of thrombin bound to cultured bovine aortic endothelial cells (BAEC) by ATIII and the effect of the inhibitor on the activation of PC has been studied using purified components of bovine origin [22].
  • Of these molecules, antithrombin III and basic fibroblast growth factor have been shown to bind to specific cell surface heparan sulfate proteoglycans [23].
  • While Heparin-Membrane Adsorber were found to isolate and concentrate the Antithrombin III efficiently, the removal of the major bovine serum proteins (albumin, transferrin, immunoglobulins) required a multistage process [24].

Analytical, diagnostic and therapeutic context of MGC127984


  1. Purification of a modified form of bovine antithrombin III as an HIV-1 CD8+ T-cell antiviral factor. Geiben-Lynn, R., Brown, N., Walker, B.D., Luster, A.D. J. Biol. Chem. (2002) [Pubmed]
  2. Antithrombin III-independent effect of depolymerized holothurian glycosaminoglycan (DHG) on acute thromboembolism in mice. Nagase, H., Kitazato, K.T., Sasaki, E., Hattori, M., Kitazato, K., Saito, H. Thromb. Haemost. (1997) [Pubmed]
  3. Assessment of interference by heparin cofactor II in the DuPont aca antithrombin-III assay. Hortin, G.L., Tollefsen, D.M., Santoro, S.A. Am. J. Clin. Pathol. (1988) [Pubmed]
  4. Anti-viral activity of human antithrombin III. Elmaleh, D.R., Brown, N.V., Geiben-Lynn, R. Int. J. Mol. Med. (2005) [Pubmed]
  5. A study of the effect of acute systemic anaphylaxis on blood coagulation and TAME esterase activity in calves. Black, W.D., Gentry, P.A. Can. J. Comp. Med. (1980) [Pubmed]
  6. Formation of a serine enzyme in the presence of bovine factor VIII (antihemophilic factor) and thrombin. Vehar, G.A., Davie, E.W. Science (1977) [Pubmed]
  7. Studies of thrombin-induced proteoglycan release in the degradation of human and bovine cartilage. Furmaniak-Kazmierczak, E., Cooke, T.D., Manuel, R., Scudamore, A., Hoogendorn, H., Giles, A.R., Nesheim, M. J. Clin. Invest. (1994) [Pubmed]
  8. Heparin inhibition of von Willebrand factor-dependent platelet function in vitro and in vivo. Sobel, M., McNeill, P.M., Carlson, P.L., Kermode, J.C., Adelman, B., Conroy, R., Marques, D. J. Clin. Invest. (1991) [Pubmed]
  9. Interaction of antithrombin III with bovine aortic segments. Role of heparin in binding and enhanced anticoagulant activity. Stern, D., Nawroth, P., Marcum, J., Handley, D., Kisiel, W., Rosenberg, R., Stern, K. J. Clin. Invest. (1985) [Pubmed]
  10. A coagulation pathway on bovine aortic segments leading to generation of Factor Xa and thrombin. Stern, D.M., Nawroth, P.P., Kisiel, W., Handley, D., Drillings, M., Bartos, J. J. Clin. Invest. (1984) [Pubmed]
  11. Crystal structure of cleaved bovine antithrombin III at 3.2 A resolution. Mourey, L., Samama, J.P., Delarue, M., Petitou, M., Choay, J., Moras, D. J. Mol. Biol. (1993) [Pubmed]
  12. The complete amino acid sequence of bovine antithrombin (ATIII). Mejdoub, H., Le Ret, M., Boulanger, Y., Maman, M., Choay, J., Reinbolt, J. J. Protein Chem. (1991) [Pubmed]
  13. An Arg-Gly-Asp sequence within thrombin promotes endothelial cell adhesion. Bar-Shavit, R., Sabbah, V., Lampugnani, M.G., Marchisio, P.C., Fenton, J.W., Vlodavsky, I., Dejana, E. J. Cell Biol. (1991) [Pubmed]
  14. The in situ inhibition of prothrombinase-formed human alpha-thrombin and meizothrombin(des F1) by antithrombin III and heparin. Schoen, P., Lindhout, T. J. Biol. Chem. (1987) [Pubmed]
  15. Inhibition of prothrombinase complex by plasma proteinase inhibitors. Ellis, V., Scully, M.F., Kakkar, V.V. Biochemistry (1984) [Pubmed]
  16. Identification in vitro of an endothelial cell surface cofactor for antithrombin III. Parallel studies with isolated perfused rat hearts and microcarrier cultures of bovine endothelium. Busch, C., Owen, W.G. J. Clin. Invest. (1982) [Pubmed]
  17. Effects of hypoxia on heparan sulfate in bovine aortic and pulmonary artery endothelial cells. Karlinsky, J.B., Rounds, S., Farber, H.W. Circ. Res. (1992) [Pubmed]
  18. Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Ny, T., Sawdey, M., Lawrence, D., Millan, J.L., Loskutoff, D.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  19. Reaction of antithrombin III with thrombin bound to the vascular endothelium. Analysis in a recirculating perfused rabbit heart preparation. Lollar, P., MacIntosh, S.C., Owen, W.G. J. Biol. Chem. (1984) [Pubmed]
  20. The effect of prothrombin fragment 2 on the inhibition of thrombin by antithrombin III. Walker, F.J., Esmon, C.T. J. Biol. Chem. (1979) [Pubmed]
  21. The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the Kunitz inhibitors. Le Bonniec, B.F., Guinto, E.R., MacGillivray, R.T., Stone, S.R., Esmon, C.T. J. Biol. Chem. (1993) [Pubmed]
  22. Formation of activated protein C and inactivation of cell-bound thrombin by antithrombin III at the surface of cultured vascular endothelial cells--a comparative study of two anticoagulant mechanisms. Delvos, U., Meusel, P., Preissner, K.T., Müller-Berghaus, G. Thromb. Haemost. (1987) [Pubmed]
  23. Specificity of lipoprotein lipase binding to endothelial cells. Stins, M.F., Sivaram, P., Sasaki, A., Goldberg, I.J. J. Lipid Res. (1993) [Pubmed]
  24. Comparison of membrane adsorber (MA) based purification schemes for the down-stream processing of recombinant h-AT III. Reif, O.W., Freitag, R. Bioseparation (1994) [Pubmed]
  25. Neutrophil elastase cleavage of human factor IX generates an activated factor IX-like product devoid of coagulant function. Samis, J.A., Kam, E., Nesheim, M.E., Giles, A.R. Blood (1998) [Pubmed]
  26. Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. Bertina, R.M., van der Linden, I.K., Mannucci, P.M., Reinalda-Poot, H.H., Cupers, R., Poort, S.R., Reitsma, P.H. J. Biol. Chem. (1990) [Pubmed]
  27. Crystallization and preliminary crystallographic data for bovine antithrombin III. Samama, J.P., Delarue, M., Mourey, L., Choay, J., Moras, D. J. Mol. Biol. (1989) [Pubmed]
  28. Studies of heparin binding to antithrombin III by crossed immunoelectrophoresis. Barrowcliffe, T.W. Thromb. Haemost. (1980) [Pubmed]
  29. Comparison of lipid binding and kinetic properties of normal, variant, and gamma-carboxyglutamic acid modified human factor IX and factor IXa. Jones, M.E., Griffith, M.J., Monroe, D.M., Roberts, H.R., Lentz, B.R. Biochemistry (1985) [Pubmed]
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