Download PDF
Thromb Haemost 1997; 78(01): 577-580
DOI: 10.1055/s-0038-1657592
Thrombin and its modulation
Schattauer GmbH Stuttgart

Modulation of Thrombin’s Procoagulant and Anticoagulant Properties

Lawrence L K Leung
1   Division of Hematology, Department of Medicine, Stanford University Medical School, Stanford, CA, USA
,
Craig S Gibbs
2   Gilead Sciences, Foster City, CA, USA
› Author Affiliations
Further Information

Publication History

Publication Date:
12 July 2018 (online)

  PDF Download  Permissions and Reprints
 

  • References

  • 1 Esmon CT. Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J 1995; 9: 946-955
    CrossrefPubMedGoogle Scholar
  • 2 Dang QD, Vindigni A, Di Cera E. An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. Proc Natl Acad Sci USA 1995; 92: 5977-5981
    CrossrefPubMedGoogle Scholar
  • 3 Wells CM, Di Cera E. Thrombin is a Na(+)-activated enzyme. Biochemistry 1992; 31: 11721-11730
    CrossrefPubMedGoogle Scholar
  • 4 Di Cera E, Guinto ER, Vindigni A, Dang QD, Ayala YM, Wuyi M, Tulinsky A. The Na+ binding site of thrombin. J Biol Chem 1995; 270: 22089-22092
    CrossrefPubMedGoogle Scholar
  • 5 Dang QD, Di Cera E. Residue 225 determines the Na+-induced allosteric regulation of catalytic activity in serine proteases. Proc Natl Acad Sci USA 1996; 93: 10653-10656
    CrossrefPubMedGoogle Scholar
  • 6 Wu Q, Sheehan JP, Tsiang M, Lentz SR, Birktoft JJ, Sadler JE. Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin. Proc Natl Acad Sci USA 1991; 88: 6775-6779
    CrossrefPubMedGoogle Scholar
  • 7 Tsiang M, Jain AK, Dunn KE, Rojas ME, Leung LLK, Gibbs CS. Functional mapping of the surface residues of thrombin. J Biol Chem 1995; 270: 16854-16863
    CrossrefPubMedGoogle Scholar
  • 8 Tsiang M, Jain AK, Gibbs CS. Functional requirements for inhibition of thrombin by antithrombin III in the presence and absence of heparin. Submitted for publication.
    PubMedGoogle Scholar
  • 9 Sheehan JP, Sadler JE. Proc Natl Acad Sci USA 1994; 91: 5518-5522
    CrossrefPubMed
  • 10 Gan ZR, Li Y, Chen Z, Lewis SD, Shafer JA. J Biol Chem. 1994; 269: 1301-1305
    PubMedGoogle Scholar
  • 11 Gibbs CS, Coutre SE, Tsiang M, Li WX, Jain AK, Dunn KE, Law VS, Mao CT, Matsumura SY, Mejza SJ, Paborsky LR, Leung LLK. Conversion of thrombin into an anticoagulant by protein engineering. Nature 1995; 378: 413-416
    CrossrefPubMedGoogle Scholar
  • 12 Tsiang M, Paborsky LR, Li WX, Jain AK, Mao CT, Dunn KE, Lee DW, Matsumura SY, Matteucci M, Coutre SE, Leung LLK, Gibbs CS. Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo. Biochemistry 1996; 35: 16449-16457
    CrossrefPubMedGoogle Scholar
  • 13 Musci G, Berliner LJ. Ligands which effect human protein C activation by thrombin. J Biol Chem 1987; 262: 13889-13891
    PubMedGoogle Scholar
  • 14 Berg DT, Wiley MR, Grinnell BW. Enhanced protein C activtion and inhibition of fibrinogen cleavage by a thrombin modulator. Science 1996; 273: 1389-1391
    CrossrefPubMedGoogle Scholar
  • 15 Solis MM, Vitti M, Cook J, Young D, Glaser C, Light D, Morser J, Wydro R, Yu S, Fink L. et al Recombinant soluble human thrombomodulin: a randomized, blinded assessment of prevention of venous thrombosis and effects on hemostatic parameters in a rat model. Thromb Res 1994; 73: 385-394
    CrossrefPubMedGoogle Scholar
  • 16 McBane RD, Wysokinski WE, Chesebro JH, Owen WG. Antithrombotic action of endogenous porcine protein C activated with a latent porcine thrombin preparation. Thromb. Haemostasis 1995; 74: 879-885
    Article in Thieme ConnectPubMedGoogle Scholar