Thrombin interactions

Chest

Volumn 124, Issue 3 SUPPL., 2003, Pages 11S-17S

  Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Anticoagulants; Blood coagulation; Thrombin; Thrombin receptors

Indexed keywords

ANTICOAGULANT AGENT; ANTITHROMBIN; ARGATROBAN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9A; HEPARIN; HIRUDIN; HIRULOG; LOW MOLECULAR WEIGHT HEPARIN; PROTEIN C; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 3; PROTEINASE ACTIVATED RECEPTOR 4; PROTHROMBIN; SERINE PROTEINASE INHIBITOR; THROMBIN; THROMBIN INHIBITOR; THROMBOMODULIN; VITAMIN K GROUP; WARFARIN;

AMINO TERMINAL SEQUENCE; BABOON; BLOOD CLOTTING; BRAIN; CARBOXY TERMINAL SEQUENCE; HUMAN; INFLAMMATION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SIDE EFFECT; THROMBOCYTOPENIA; THROMBOSIS;

EID: 0141484541     PISSN: 00123692     EISSN: None     Source Type: Journal    
DOI: 10.1378/chest.124.3_suppl.11S     Document Type: Article

References (68)

1. Krem MM, Di Cera E. Molecular markers of serine protease evolution. EMBO J 2001; 20:3036-3045
2. Krem MM, Di Cera E. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem Sci 2002; 27:67-74
3. Adema CM, Hertel LA, Miller RD, et al. A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection. Proc Natl Acad Sci U S A 1997; 94:8691-8696
4. Cohen J. The immunopathogenesis of sepsis. Nature 2002; 420:885-891
5. Tauszig S, Jouanguy E, Hoffmann JA, et al. Toll-related receptors and the control of antimicrobial peptide expression in Drosophila. Proc Natl Acad Sci U S A 2000; 97:10520-10525
6. Sun WY, Witte DP, Degen JL, et al. Prothrombin deficiency results in embryonic and neonatal lethality in mice. Proc Natl Acad Sci U S A 1998; 95:7597-7602
7. Xue J, Wu Q, Westfield LA, et al. Incomplete embryonic lethality and fatal neonatal hemorrhage caused by prothrombin deficiency in mice. Proc Natl Acad Sci U S A 1998; 95:7603-7607
8. Coughlin SR. Thrombin signalling and protease-activated receptors. Nature 2000; 407:258-264
9. Suh TT, Holmback K, Jensen NJ, et al. Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen-deficient mice. Genes Dev 1995; 9:2020-2033
10. Dihanich M, Kaser M, Reinhard E, et al. Prothrombin mRNA is expressed by cells of the nervous system. Neuron 1991; 6:575-581
11. Kaufmann R, Junker U, Junker K, et al. The serine proteinase thrombin promotes migration of human renal carcinoma cells by a PKA-dependent mechanism. Cancer Lett 2002; 180: 183-190
12. Stenina OI. Regulation of gene expression in vascular cells by coagulation proteins. Curr Drug Targets 2003; 4:143-158
13. Libby P. Inflammation in atherosclerosis. Nature 2002; 420: 868-874
14. Donovan FM, Cunningham DD. Signaling pathways involved in thrombin-induced cell protection. J Biol Chem 1998; 273:12746-12752
15. Chinni C, de Niese MR, Tew DJ, et al. Thrombin, a survival factor for cultured myoblasts. J Biol Chem 1999; 274:9169-9174
16. Bizios R, Lai L, Fenton JW II, et al. Thrombin-induced chemotaxis and aggregation of neutrophils. J Cell Physiol 1986; 128:485-490
17. Bar-Shavit R, Kahn A, Wilner GD, et al. Monocyte chemotaxis: stimulation by specific exosite region in thrombin. Science 1983; 220:728-731
18. Zhou H, Gabazza EC, Takeya H, et al. Prothrombin and its derivatives stimulate motility of melanoma cells. Thromb Haemost 1998; 80:407-412
19. Mann KG, Butenas S, Brummel K. The dynamics of thrombin formation. Arterioscler Thromb Vasc Biol 2003; 23:17-25
20. Griffin JH. Blood coagulation: the thrombin paradox. Nature 1995; 378:337-338
21. Taylor FB Jr, Peer GT, Lockhart MS, et al. Endothelial cell protein C receptor plays an important role in protein C activation in vivo. Blood 2001; 97:1685-1688
22. Esmon CT. Regulation of blood coagulation. Biochim Biophys Acta 2000; 1477:349-360
23. Olson ST, Chuang YJ. Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases. Trends Cardiovasc Med 2002; 12:331-338
24. O'Brien PJ, Molino M, Kahn M, et al. Protease activated receptors: theme and variations. Oncogene 2001; 20:1570-1581
25. Cottrell GS, Coelho AM, Bunnett NW. Protease-activated receptors: the role of cell-surface proteolysis in signalling. Essays Biochem 2002; 38:169-183
26. Vu TK, Wheaton VI, Hung DT, et al. Domains specifying thrombin-receptor interaction. Nature 1991; 353:674-677
27. Ishihara H, Connolly AJ, Zeng D, et al. Protease-activated receptor 3 is a second thrombin receptor in humans. Nature 1997; 386:502-506
28. Kahn ML, Zheng YW, Huang W, et al. A dual thrombin receptor system for platelet activation. Nature 1998; 394: 690-694
29. Xu WF, Andersen H, Whitmore TE, et al. Cloning and characterization of human protease-activated receptor 4. Proc Natl Acad Sci U S A 1998; 95:6642-6646
30. Andersen H, Greenberg DL, Fujikawa K, et al. Protease-activated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity. Proc Natl Acad Sci U S A 1999; 96:11189-11193
31. van Holde KE. A hypothesis concerning diffusion-limited protein-ligand interactions. Biophys Chem 2002; 101-102, 249-254
32. Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 1996; 271:16603-16608
33. Bode W, Turk D, Karshikov A. The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1992; 1:426-471
34. Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann N Y Acad Sci 2001; 936:11-30
35. Rose T, Di Cera E. Three-dimensional modeling of thrombin-fibrinogen interaction. J Biol Chem 2002; 277:18875-18880
36. Rydel TJ, Tulinsky A, Bode W, et al. Refined structure of the hirudin-thrombin complex. J Mol Biol 1991; 221:583-601
37. Mathews TJ, Padmanabhan KP, Ganesh V, et al. Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Biochemistry 1994; 33:3266-3279
38. Ayala YM, Cantwell AM, Rose T, et al. Molecular mapping of thrombin-receptor interactions. Proteins 2001; 45:107-116
39. Pineda AO, Cantwell AM, Bush LA, et al. The thrombin epitope recognizing thrombomodulin is a highly cooperative hot spot in exosite I. J Biol Chem 2002; 277:32015-32019
40. Fuentes-Prior P, Iwanaga Y, Huber R, et al. Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex. Nature 2000; 404:518-525
41. Tsiang M, Jain AK, Dunn KE, et al. Functional mapping of the surface residues of human thrombin. J Biol Chem 1995; 270:16854-16863
42. Hall SW, Nagashima M, Zhao L, et al. Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 1999; 274:25510-25516
43. Tsiang M, Jain AK, Gibbs CS. Functional requirements for inhibition of thrombin by antithrombin III in the presence and absence of heparin. J Biol Chem 1997; 272:12024-12029
44. Sheehan JP, Sadler JE. Molecular mapping of the heparin-binding exosite of thrombin. Proc Natl Acad Sci U S A 1994; 91:5518-5522
45. van Boven HH, Lane DA. Antithrombin and its inherited deficiency states. Semin Hematol 1997; 34:188-204
46. Ishiguro K, Kojima T, Kadomatsu K, et al. Complete antithrombin deficiency in mice results in embryonic lethality. J Clin Invest 2000; 106:873-878
47. Sheehan JP, Tollefsen DM, Sadler JE. Heparin cofactor II is regulated allosterically and not primarily by template effects: studies with mutant thrombins and glycosaminoglycans. J Biol Chem 1994; 269:32747-32751
48. Di Cera E, Guinto ER, Vindigni A, et al. The Na+ binding site of thrombin. J Biol Chem 1995; 270:22089-22092
49. Dang OD, Vindigni A, Di Cera E. An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. Proc Natl Acad Sci U S A 1995; 92:5977-5981
50. 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; 276:25143-25149
51. Myles T, Yun TH, Leung LL. Structural requirements for the activation of human factor VIII by thrombin. Blood 2002; 100:2820-2826
52. Henriksen RA, Dunham CK, Miller LD, et al. Prothrombin Greenville, Arg517->Gln, identified in an individual heterozygous for dysprothrombinemia. Blood 1998; 91:2026-2031
53. 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; 85:651-654
54. Adrogue HJ, Madias NE. Hypernatremia. N Engl J Med 2000; 342:1581-1589
55. Adrogue HJ, Madias NE. Hypernatremia. N Engl J Med 2000; 342:1493-1499
56. Goldman JA, Eckerling B. Intracranial dural sinus thrombosis following intrauterine instillation of hypertonie saline. Am J Obstet Gynecol 1972; 112:1132-1133
57. Grant PJ, Tate GM, Hughes JR, et al. Does hypernatraemia promote thrombosis? Thromb Res 1985; 40:393-399
58. Rubin D, Christian C. Retinal hemorrhages in infants with hyponatremic seizures. Pediatr Emerg Care 2001; 17:313-314
59. Rezaie AR, He X. Sodium binding site of factor Xa: role of sodium in the prothrombinase complex. Biochemistry 2000; 39:1817-1825
60. Petrovan RJ, Ruf W. Role of residue Phe225 in the cofactor-mediated, allosteric regulation of the serine protease coagulation factor VIIa. Biochemistry 2000; 39:14457-14463
61. He X, Rezaie AR. Identification and characterization of the sodium-binding site of activated protein C. J Biol Chem 1999; 274:4970-4976
62. Hirsh J, Weitz JI. New antithrombotic agents. Lancet 1999; 353:1431-1436
63. Weitz JI. Low-molecular-weight heparins. N Engl J Med 1997; 337:688-698
64. Richardson JL, Kroger B, Hoeffken W, et al. Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. EMBO J 2000; 19:5650-5660
65. Pineda AO, Savvides SN, Waksman G, et al. Crystal structure of the anticoagulant slow form of thrombin. J Biol Chem 2002; 277:40177-40180
66. Hanson SR, Griffin JH, Harker LA, et al. Antithrombotic effects of thrombin-induced activation of endogenous protein C in primates. J Clin Invest 1993; 92:2003-2012
67. Gibbs CS, Coutre SE, Tsiang M, et al. Conversion of thrombin into an anticoagulant by protein engineering. Nature 1995; 378:413-416
68. Gruber A, Cantwell AM, Di Cera E, et al. The thrombin mutant W215A/E217A shows safe and potent anticoagulant and antithrombotic effects in vivo. J Biol Chem 2002; 277:27581-27584