Is Na+ a coagulation factor?

Thrombosis and Haemostasis

Volumn 95, Issue 6, 2006, Pages 920-921

  Page, Michael J ^a   Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 8A; BLOOD CLOTTING FACTOR 9A; CHROMOGENIC SUBSTRATE; FIBRINOGEN; PHENYLALANINE; PROLINE; SERINE PROTEINASE; SODIUM ION; THROMBIN; TYROSINE;

BINDING SITE; BLOOD CLOTTING; COMPLEX FORMATION; EDITORIAL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; MOLECULAR MIMICRY; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; SODIUM BLOOD LEVEL;

BINDING SITES; BLOOD COAGULATION; BLOOD COAGULATION FACTORS; FACTOR IXA; FACTOR VIIA; HUMANS; PROTEIN BINDING; PROTEIN CONFORMATION; SODIUM; THROMBIN;

EID: 33745293025     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH06-05-0239     Document Type: Editorial

References (34)

1. Page MJ, Di Cera E. Role of Na+ and K+ in enzyme function. Physiol Rev 2006, in press.
2. Orthner CL, Kosow DP. The effect of metal ions on the amidolytic acitivity of human factor Xa (activated Stuart-Prower factor). Arch Biochem Biophys 1978; 185: 400-6.
3. Orthner CL, Kosow DP. Evidence that human alpha-thrombin is a monovalent cation-activated enzyme. Arch Biochem Biophys 1980; 202: 63-75.
4. Steiner SA, Amphlett GW, Castellino FJ. Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations. Biochem Biophys Res Commun 1980; 94: 340-7.
5. Steiner SA, Castellino FJ. Kinetic mechanism for stimulation by monovalent cations of the amidase activity of the plasma protease bovine activated protein C. Biochemistry 1985; 24: 609-17.
6. Wells CM, Di Cera E. Thrombin is a Na(+)-activated enzyme. Biochemistry 1992; 31: 11721-30.
7. Di Cera E, Guinto ER, Vindigni A, et al. The Na+ binding site of thrombin. J Biol Chem 1995; 270: 22089-92.
8. Dang OD, Vindigni A, Di Cera E. An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. Proc Natl Acad Sci USA 1995; 92: 5977-81.
9. Ayala YM, Cantwell AM, Rose T, et al. Molecular mapping of thrombin-receptor interactions. Proteins 2001; 45: 107-16.
10. Myles T, Yun TH, Hall SW, et al. An extensive interaction interface between thrombin and factor V is required for factor V activation. J Biol Chem 2001; 276: 25143-9.
11. Nogami K, Zhou Q, Myles T, et al. Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain. J Biol Chem 2005; 280: 18476-87.
12. Yun TH, Baglia FA, Myles T, et al. Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively. J Biol Chem 2003; 278: 48112-9.
13. 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: 10653-6.
14. Gopalakrishna K, Rezaie AR. The influence of sodium ion binding on factor IXa activity. Thromb Haemost 2006; 95: 936-41.
15. Rezaie AR, He X. Sodium binding site of factor Xa: role of sodium in the prothrombinase complex. Biochemistry 2000, 39: 1817-25.
16. Schmidt AE, Stewart JE, Mathur A, et al. Na+ site in blood coagulation factor IXa: effect on catalysis and factor VIIIa binding. J Mol Biol 2005; 350: 78-91.
17. Monnaie D, Arosio D, Griffon N, et al. Identification of a binding site for quaternary amines in factor Xa. Biochemistry 2000; 39: 5349-54.
18. Underwood MC, Zhong D, Mathur A, et al. Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human coagulation factor xa. Studies on catalytic efficiency and inhibitor binding. J Biol Chem 2000; 275: 36876-84.
19. Camire, RM Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J Biol Chem 2002; 277: 37863-70.
20. Petrovan RJ, Ruf W. Role of residue Phe225 in the cofactor-mediated, allosteric regulation of the serine protease coagulation factor VIIa. Biochemistry 2000; 39: 14457-63.
21. Pineda AO, Carrell CJ, Bush LA, et al. Molecular dissection of Na+ binding to thrombin. J Biol Chem 2004; 279: 31842-53.
22. Di Cera E. Thrombin interactions. Chest 2003; 124: 11S-17S.
23. Mann KG. Thrombin formation. Chest 2003; 124: 4S-10S.
24. Adrogue HJ, Madias NE. Hypernatremia. N Engl J Med 2000; 342: 1493-9.
25. Adrogue HJ, Madias NE. Hyponatremia. N Engl J Med 2000; 342: 1581-9.
26. Grant PJ, Tate GM, Hughes JR. Does hypernatraemia promote thrombosis? Thromb Res 1985; 40: 393-9.
27. Almond CS, Shin AY, Fortescue EB, et al. Hyponatremia among runners in the Boston Marathon. N Engl J Med 2005; 352: 1550-6.
28. Degen SJ, McDowell SA, Sparks LM, et al. Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala. Thromb Haemost 1995; 73: 203-9.
29. Miyata T, Aruga R, Umeyama H, et al. Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry 1992; 31: 7457-62.
30. Henriksen RA, Dunham CK, Miller LD, et al. Prothrombin Greenville, Arg517-->Gln, identified in an individual heterozygous for dysprothrombinemia. Blood 1998; 91: 2026-31.
31. Sun WY, Smirnow D, Jenkins ML, et al. Prothrombin Scranton: substitution of an amino acid residue involved in the binding of Na+ (LYS-556 to THR) leads to dysprothrombinemia. Thromb Haemost 2001; 85: 651-4.
32. Stanchev H, Philips M, Villoutreix BO, et al. Prothrombin deficiency caused by compound heterozigosity for two novel mutations in the prothrombin gene associated with a bleeding tendency. Thromb Haemost 2006; 95: 195-8.
33. Rouy S, Vidaud D, Alessandri JL, et al. Prothrombin Saint-Denis: a natural variant with a point mutation resulting in Asp to Glu substitution at position 552 in prothrombin. Br J Haematol 2006; 132: 770-3.
34. Bush LA, Nelson RW, Di Cera E. Murine thrombin lacks Na+ activation but retains high catalytic activity. J Biol Chem 2006; 281: 7183-8.