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Thromb Haemost 2009; 102(03): 421-423
DOI: 10.1160/TH09-08-0050
Editorial Focus
Schattauer GmbH

Prothrombinase complexes with different physiological roles

Martin F. Lavin
1   Queensland Institute of Medical Research, Radiation Biology and Oncology, Brisbane Queensland, Australia
2   The University of Queensland Centre for Clinical Research, Brisbane Queensland, Australia
,
Paul P. Masci
3   Centre for Integrative Clinical and Molecular Medicine, School of Medicine, Southern Region, Faculty of Health Sciences, University of Queensland, Brisbane Queensland, Australia
› Author Affiliations
Further Information

Publication History

Received: 11 August 2009

Accepted: 11 August 2009

Publication Date:
22 November 2017 (online)

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  • References

  • 1 Masci PP, Whitaker AN, de Jersey J. Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis. Biochem 1988; 17: 825-835.
    PubMedGoogle Scholar
  • 2 Kini RM. The intriguing world of prothrombin activators from snake venom. Toxicon 2005; 45: 1133-1145.
    CrossrefPubMedGoogle Scholar
  • 3 Joseph JS, Chung MC, Jyeaseelan K, Kini RM. Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa. Blood 1999; 94: 621-631.
    PubMedGoogle Scholar
  • 4 St Pierre L, Masci PP, Filippovich I. et al. Comparative analysis of prothrombin activators from the venom of Australian elapids Mol Biol Evol 2005; 22: 1853-1864.
    CrossrefPubMed
  • 5 Kwong S, Woods AE, Mirtschin PJ. et al. The Recruitment of Blood Coagulation Factor X into Snake Venom Gland as a Toxin: The Role of Promoter Cis-elements in Its Expression. Thromb Haemost 2009; 469-478.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 6 Bos MH, Boltz M, St Pierre L. et al. Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptions. Blood 2009; 114: 686-692.
    CrossrefPubMedGoogle Scholar
  • 7 Rao VS, Swarup S, Kini RM. The nonenzymatic subunit of pseutarin C, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom, shows structural similarity to mammalian coagulation factor V. Blood 2003; 102: 1347-1354.
    CrossrefPubMedGoogle Scholar
  • 8 Rao VS, Swarup S, Kini RM. The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa. J Thromb Haemost 2004; 92: 509-521.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 9 Reza MA, Minh LT, Swarup S, Kini RM. Molecular evolution caught in action: gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake). J Thromb Haemost 2006; 04: 1346-1353.
    CrossrefPubMedGoogle Scholar
  • 10 Reza MA, Swarup S, Kini RM. Structure of two genes encoding parallel prothrombin activators in Tropidechis carinatus snake: gene duplication and recruitment of factor X gene to the venom gland. J Thromb Haemost 2007; 05: 117-126.
    CrossrefPubMedGoogle Scholar
  • 11 Masci PP. PhD Thesis. Studies of coagulation and fibrinolysis using Australian snake venoms: From molecular toxinology to novel therapeutic agents. 2000
    PubMedGoogle Scholar
  • 12 Masci PP, Tibbals J. Genus Pseudonaja from snakes. In The Biology of Australian Snakes. Sutherland SK and Tibballs J. Ed. Oxford University Press; 2001: 99-129.
    Google Scholar
  • 13 Fry BG, Scheib H, van der WL. et al. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). Mol Cell Proteomics 2008; 07: 215-246.
    CrossrefPubMedGoogle Scholar
  • 14 Tibballs J, Sutherland SK, Rivera R. et al. The cardiovascular and haematological effects of purified prothrombin activator from the common brown snake (Pseudonaja textilis) and their antagonism with heparin. Anaesth Intensive Care 1992; 20: 28-32.
    PubMedGoogle Scholar
  • 15 Bode J, Kohwi Y, Dickinson L. et al. Biological significance of unwinding capability of nuclear matrix-associating DNAs. Science 1992; 25: 257-290.
    PubMedGoogle Scholar
  • 16 van Drunen CM, Oosterling RW, Keultjes GM. et al. Analysis of the chromatin domain organization around the plastocyanin gene reveals an MAR-specific sequence element in Arabidopsis thaliana. Nucleic Acids Res 1997; 25: 3904-3911.
    CrossrefPubMedGoogle Scholar
  • 17 Mann KG, Kalafatis M. Factor V: A combination of Dr Jekyll and Mr Hyde. Blood 2003; 101: 20-30.
    CrossrefPubMedGoogle Scholar
  • 18 Tozo R, Camire RM. Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J Biol Chem 2004; 279: 21643-21650.
    CrossrefPubMedGoogle Scholar
  • 19 Zhu H, Toso R, Camire RM. Inhibitory sequences within the B-domain stabilize circulating factor V in an inactive state. J Biol Chem 2007; 282: 15033-15039.
    CrossrefPubMedGoogle Scholar
  • 20 Esmon CT. The protein C pathway. Chest 2003; 124 (Suppl. 03) 26S-32S.
    CrossrefPubMedGoogle Scholar
  • 21 Masci PP, Rowe EA, Whitaker AN. et al. Fibrinolysis as a feature of disseminated intravascular coagulation (DIC) after Pseudonaja textilis textilis envenomation. Thromb Res 1990; 59: 859-870.
    CrossrefPubMedGoogle Scholar