Congenital prothrombin deficiency

Seminars in Thrombosis and Hemostasis

Volumn 35, Issue 4, 2009, Pages 367-381

  Lancellotti, Stefano ^a   De Cristofaro, Raimondo ^a  

^a CATHOLIC UNIVERSITY   (Italy)

Author keywords

Coagulation; Congenital bleeding diseases; Hemorrhagic disorders; Prothrombin deficiency; Thrombin

Indexed keywords

ANTIFIBRINOLYTIC AGENT; BEBULIN VH; BERIPLEX P N; FRESH FROZEN PLASMA; OCTAPLEX; ORAL CONTRACEPTIVE AGENT; PROPLEX T; PROTHROMBIN; PROTHROMBIN COMPLEX; PROTHROMBINEX HT; PROTHROMPLEX T; PROTHRORAAS; SODIUM ION; THROMBIN; UMAN; UNCLASSIFIED DRUG;

BLEEDING TENDENCY; BLOOD LEVEL; CLINICAL FEATURE; DYSPROTHROMBINEMIA; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE DELETION; HUMAN; HYPOPROTHROMBINEMIA; MENORRHAGIA AND METRORRHAGIA; MISSENSE MUTATION; NONSENSE MUTATION; PARTIAL THROMBOPLASTIN TIME; PHENOTYPE; PLASMA TRANSFUSION; PRIORITY JOURNAL; PROTHROMBIN DEFICIENCY; PROTHROMBIN TIME; REVIEW; STOP CODON;

AMINO ACID SEQUENCE; ANTIFIBRINOLYTIC AGENTS; BLOOD COAGULATION FACTORS; ENDOPEPTIDASES; FEMALE; HEMORRHAGE; HETEROZYGOTE; HUMANS; HYPOPROTHROMBINEMIAS; LABORATORY TECHNIQUES AND PROCEDURES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PREOPERATIVE CARE; PROTHROMBIN; THROMBIN; VIPER VENOMS;

EID: 67749084428     PISSN: 00946176     EISSN: 10989064     Source Type: Journal    
DOI: 10.1055/s-0029-1225759     Document Type: Review

References (98)

1. Barnhart MI. Cellular site for prothrombin synthesis. Am J Physiol 1960;199:360-366
2. Esmon CT. Regulation of blood coagulation. Biochim Biophys Acta 2000;1477:349-360
3. Mosesson MW. Fibrinogen and fibrin structure and functions. J Thromb Haemost 2005;3:1894-1904
4. Segers K, Dahlbäck B, Bock PE, Tans G, Rosing J, Nicolaes GA. The role of thrombin exosites I and II in the activation of human coagulation factor V. J Biol Chem 2007;282:33915-33924 (Pubitemid 350159447)
5. Myles T, Yun TH, Leung LL. Structural requirements for the activation of human factor VIII by thrombin. Blood 2002;100:2820-2826
6. Isetti G, Maurer MC. Employing mutants to study thrombin residues responsible for factor XIII activation peptide recognition: a kinetic study. Biochemistry 2007;46:2444-2452 (Pubitemid 46362418)
7. Bar-Shavit R, Kahn AJ, Mann KG, Wilner GD. Identification of a thrombin sequence with growth factor activity on macrophages. Proc Natl Acad Sci U S A 1986;83:976-980 (Pubitemid 16086396)
8. Zetter BR, Antoniades HN. Stimulation of human vascular endothelial cell growth by a platelet-derived growth factor and thrombin. J Supramol Struct 1979;11:361-370 (Pubitemid 10069147)
9. Seino Y, Ikeda U, Ikeda M, et al. Interleukin 6 gene transcripts are expressed in human atherosclerotic lesions. Cytokine 1994;6:87-91 (Pubitemid 24120205)
10. Fenton JW II. Regulation of thrombin generation and functions. Semin Thromb Hemost 1988;14:234-240
11. Hu L, Roth JM, Brooks P, Luty J, Karpatkin S. Thrombin up-regulates cathepsin D which enhances angiogenesis, growth, and metastasis. Cancer Res 2008;68:4666-4673
12. Degen SJ, Davie EW. Nucleotide sequence of the gene for human prothrombin. Biochemistry 1987;26:6165-6177 (Pubitemid 17153322)
13. Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL. Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively. Somat Cell Mol Genet 1987;13:285-292
14. Stanchev H, Philips M, Villoutreix BO, Aksglaede L, Lethagen S, Thorsen S. Prothrombin deficiency caused by compound heterozygosity for two novel mutations in the prothrombin gene associated with a bleeding tendency. Thromb Haemost 2006;95:195-198
15. Akhavan S, Mannucci PM, Lak M, et al. Identification and three-dimensional structural analysis of nine novel mutations in patients with prothrombin deficiency. Thromb Haemost 2000;84:989-997 (Pubitemid 32014034)
16. Peyvandi F, Duga S, Akhavan S, Mannucci PM. Rare coagulation deficiencies. Haemophilia 2002;8:308-321
17. Mannucci PM, Duga S, Peyvandi F. Recessively inherited coagulation disorders. Blood 2004;104:1243-1252
18. Acharya SS, Coughlin A, Dimichele D; MNorth American Rare Bleeding Disorder Study Group. Rare Bleeding Disorder Registry: deficiencies of factors II, V, VII, X, XIII, fibrinogen and dysfibrinogenemias. J Thromb Haemost 2004;2:248-256
19. Girolami A, Scarano L, Saggiorato G, Girolami B, Bertomoro A, Marchiori A. Congenital deficiencies and abnormalities of prothrombin. Blood Coagul Fibrinolysis 1998;9:557-569
20. Klaus C, Plaimauer B, Studt JD, et al. Epitope mapping of ADAMTS13 autoantibodies in acquired thrombotic thrombocytopenic purpura. Blood 2004;103:4514-4519 (Pubitemid 38745978)
21. Peyvandi F, Cattaneo M, Inbal A, De Moerloose P, Spreafico M. Rare bleeding disorders. Haemophilia 2008;14(Suppl 3):202-210
22. 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 (Pubitemid 28293298)
23. 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 (Pubitemid 28293299)
24. Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S, Itakura M. Molecular and genetic analysis of a compound heterozygote for dysprothrombinemia of prothrombin Tokushima and hypoprothrombinemia. Am J Hum Genet 1992;51:1386-1395 (Pubitemid 23001098)
25. Wang W, Fu Q, Zhou R, et al. Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly. Haemophilia 2004;10:94-97 (Pubitemid 38195632)
26. Shapiro SS, McCord S. Prothrombin. Prog Hemost Thromb 1978;4:177-209
27. Lanchantin GF, Hart DW, Friedmann JA, Saavedra NV, Mehl JW. Amino acid composition of human plasma prothrombin. J Biol Chem 1968;243:5479-5485
28. Neurath H. Evolution of proteolytic enzymes. Science 1984;224:350-357
29. Gilbert W. Genes-in-pieces revisited. Science 1985;228:823-824
30. Patthy L. Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 1985;41:657-663
31. Bányai L, Váradi A, Patthy L. Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator. FEBS Lett 1983;163:37-41
32. Bode W, Turk D, Karshikov A. The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1992;1:426-471 (Pubitemid 23016868)
33. Hageman TC, Endres GF, Scheraga HA. Mechanism of action of thrombin on fibrinogen. On the role of the A chain of bovine thrombin in specificity and in differentiating between thrombin and trypsin. Arch Biochem Biophys 1975;171:327-336
34. DiBella EE, Maurer MC, Scheraga HA. Expression and folding of recombinant bovine prethrombin-2 and its activation to thrombin. J Biol Chem 1995;270:163-169
35. Akhavan S, Rocha E, Zeinali S, Mannucci PM. Gly319 - > arg substitution in the dysfunctional prothrombin Segovia. Br J Haematol 1999;105:667-669 (Pubitemid 29277022)
36. Lefkowitz JB, Haver T, Clarke S, et al. The prothrombin Denver patient has two different prothrombin point mutations resulting in Glu-300 - > Lys and Glu-309 - > Lys substitutions. Br J Haematol 2000;108:182-187 (Pubitemid 30089951)
37. Sun WY, Burkart MC, Holahan JR, Degen SJ. Prothrombin San Antonio: a single amino acid substitution at a factor Xa activation site (Arg320 to His) results in dysprothrombinemia. Blood 2000;95:711-714
38. Wells CM, Di Cera E. Thrombin is a Na(+)-activated enzyme. Biochemistry 1992;31:11721-11730
39. Di Cera E, Dang QD, Ayala YM. Molecular mechanisms of thrombin function. Cell Mol Life Sci 1997;53:701-730
40. Rose T, Di Cera E. Three-dimensional modeling of thrombin-fibrinogen interaction. J Biol Chem 2002;277:18875-18880
41. Pechik I, Madrazo J, Mosesson MW, Hernandez I, Gilliland GL, Medved L. Crystal structure of the complex between thrombin and the central "E" region of fibrin. Proc Natl Acad Sci U S A 2004;101:2718-2723
42. Mathews II, 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 (Pubitemid 24112639)
43. Esmon CT, Lollar P. Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII. J Biol Chem 1996;271:13882-13887 (Pubitemid 26185435)
44. 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 (Pubitemid 30186897)
45. Sheehan JP, Wu Q, Tollefsen DM, Sadler JE. Mutagenesis of thrombin selectively modulates inhibition by serpins heparin cofactor II and antithrombin III. Interaction with the anion-binding exosite determines heparin cofactor II specificity. J Biol Chem 1993;268:3639-3645 (Pubitemid 23071008) (Pubitemid 23968578)
46. Stone SR, Braun PJ, Hofsteenge J. Identification of regions of alpha-thrombin involved in its interaction with hirudin. Biochemistry 1987;26:4617-4624 (Pubitemid 17129290)
47. Akhavan S, De Cristofaro R, Peyvandi F, Lavoretano S, Landolfi R, Mannucci PM. Molecular and functional characterization of a natural homozygous Arg67His mutation in the prothrombin gene of a patient with a severe procoagulant defect contrasting with a mild hemorrhagic phenotype. Blood 2002;100:1347-1353 (Pubitemid 34864291)
48. 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 Int 1988;17:825-835
49. Van Creveld S. Congenital idiopathic hypoprothrombinemia. Acta Paediatr Suppl 1954;43:245-255
50. Huntington JA. Molecular recognition mechanisms of thrombin. J Thromb Haemost 2005;3:1861-1872
51. De Cristofaro R, Akhavan S, Altomare C, Carotti A, Peyvandi F, Mannucci PM. A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin. J Biol Chem 2004;279:13035-13043 (Pubitemid 38445881)
52. De Cristofaro R, Carotti A, Akhavan S, et al. The natural mutation by deletion of Lys9 in the thrombin A-chain affects the pKa value of catalytic residues, the overall enzyme's stability and conformational transitions linked to Na + bind-binding. FEBS J 2006;273:159-169
53. François D, Chevreaud C, Vignon D, de Mazancourt P. Prothrombin Suresnes: a case of homozygous F299V mutation responsible for hypodysprothrombinemia. Haematologica 2006;91:431-432
54. Liu CC, Brustad E, Liu W, Schultz PG. Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin. J Am Chem Soc 2007;129:10648-10649 (Pubitemid 350067462)
55. O'Marcaigh AS, Nichols WL, Hassinger NL, et al. Genetic analysis and functional characterization of prothrombins Corpus Christi (Arg382-Cys), Dhahran (Arg271-His), and hypoprothrombinemia. Blood 1996;88:2611-2618
56. Miyata T, Zheng YZ, Kato A, Kato H. A point mutation (Arg271 - > Cys) of a homozygote for dysfunctional prothrombin, prothrombin Obihiro, which has a region of high sequence variability. Br J Haematol 1995;90:688-692
57. Lechler E. Use of prothrombin complex concentrates for prophylaxis and treatment of bleeding episodes in patients with hereditary deficiency of prothrombin, factor VII, factor X, protein C protein S, or protein Z. Thromb Res 1999;95(4, Suppl 1):S39-S50 (Pubitemid 29461047)
58. Owen CA Jr, Henriksen RA, McDuffie FC, Mann KG. Prothrombin Quick. A newly identified dysprothrombinemia. Mayo Clin Proc 1978;53:29-33
59. Gill FM, Shapiro SS, Schwartz E. Severe congenital hypoprothrombinemia. J Pediatr 1978;93:264-266
60. Pabinger I, Brenner B, Kalina U, Knaub S, Nagy A, Ostermann H; Beriplex P/N Anticoagulation Reversal Study Group. Prothrombin complex concentrate (Beriplex P/N) for emergency anticoagulation reversal: a prospective multinational clinical trial. J Thromb Haemost 2008;6:622-631
61. Poort SR, Landolfi R, Bertina RM. Compound heterozygosity for two novel missense mutations in the prothrombin gene in a patient with a severe bleeding tendency. Thromb Haemost 1997;77:610-615 (Pubitemid 27182950)
62. Marchiori A, Mosena L, Prins MH, Prandoni P. The risk of recurrent venous thromboembolism among heterozygous carriers of factor V Leiden or prothrombin G20210A mutation. A systematic review of prospective studies. Haematologica 2007;92:1107-1114
63. Girolami A, Santarossa L, Scarparo P, Candeo N, Girolami B. True congenital prothrombin deficiency due to a 'new' mutation in the pre-propeptide (ARG-39 GLN). Acta Haematol 2008;120:82-86
64. Wong AY, Hewitt J, Clarke BJ, et al. Severe prothrombin deficiency caused by prothrombin-Edmonton (R-4Q) combined with a previously undetected deletion. J Thromb Haemost 2006;4:2623-2628 (Pubitemid 44741558)
65. Strijks E, Poort SR, Renier WO, Gabreëls FJ, Bertina RM. Hereditary prothrombin deficiency presenting as intracranial haematoma in infancy. Neuropediatrics 1999;30:320-324 (Pubitemid 30088324)
66. Poort SR, Michiels JJ, Reitsma PH, Bertina RM. Homozygosity for a novel missense mutation in the prothrombin gene causing a severe bleeding disorder. Thromb Haemost 1994;72:819-824
67. Sun WY, Ruiz-Saez A, Burkart MC, Bosch N, Degen SJ. Prothrombin carora: hypoprothrombinaemia caused by substitution of Tyr-44 by Cys. Br J Haematol 1999;105:670-672 (Pubitemid 29277023)
68. Board PG, Shaw DC. Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site. Br J Haematol 1983;54:245-254
69. James HL, Kim DJ, Zheng DQ, Girolami A. Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site. Blood Coagul Fibrinolysis 1994;5:841-844 (Pubitemid 24366381)
70. Morishita E, Saito M, Kumabashiri I, Asakura H, Matsuda T, Yamaguchi K. Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337 - > Thr and Arg-388 - > His). Blood 1992;80:2275-2280
71. Tamary H, Surrey S, Augustine J, Shalmon L, Schwartz E, Rappaport EF. Molecular analysis of a compound heterozygote for hypoprothrombinemia and dysprothrombinemia (-G 7248/7249 and ARG 340 TRP). Blood Coagul Fibrinolysis 1997;8:337-343 (Pubitemid 27428531)
72. Jayandharan G, Viswabandya A, Baidya S, et al. Molecular genetics of hereditary prothrombin deficiency in Indian patients: identification of a novel Ala362 - > Thr (Prothrombin Vellore 1) mutation. J Thromb Haemost 2005;3:1446-1453 (Pubitemid 41725202)
73. Henriksen RA, Owen WG, Nesheim ME, Mann KG. Identification of a congenital dysthrombin, thrombin Quick. J Clin Invest 1980;66:934-940
74. Girolami A, Coccheri S, Palareti G, Poggi M, Burul A, Cappellato G. Prothrombin Molise: a "new" congenital dysprothrombinemia, double heterozygosis with an abnormal prothrombin and "true" prothrombin deficiency. Blood 1978;52:115-125
75. Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S, Itakura M. Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia. Int J Hematol 1992;55:93-100
76. Lefkowitz JB, Weller A, Nuss R, Santiago-Borrero PJ, Brown DL, Ortiz IR. A common mutation, Arg457 - > Gln, links prothrombin deficiencies in the Puerto Rican population. J Thromb Haemost 2003;1:2381-2388
77. Kling SJ, Jones KA, Rodgers GM. A second case of prothrombin Puerto Rico I in the United States. Am J Hematol 2007;82:661-662
78. Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S. Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry 1992;31:7457-7462
79. Henriksen RA, Dunham CK, Miller LD, et al. Prothrombin Greenville, Arg517 - > Gln, identified in an individual heterozygous for dysprothrombinemia. Blood 1998;91:2026-2031
80. Sekine O, Sugo T, Ebisawa K, et al. Substitution of Gly-548 to Ala in the substrate binding pocket of prothrombin Perijá leads to the loss of thrombin proteolytic activity. Thromb Haemost 2002;87:282-287 (Pubitemid 34139866)
81. Sun WY, Smirnow D, Jenkins ML, Degen SJ. 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
82. Henriksen RA, Mann KG. Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity. Biochemistry 1989;28:2078-2082
83. Poort SR, Njo KT, Vos HL, Bertina RM. Two novel mutations in the prothrombin gene cause severe bleeding in a compound heterozygous patient. Blood Coagul Fibrinolysis 1998;9:761-764 (Pubitemid 29144982)
84. Shapiro SS, Martinez J, Holburn RR. Congenital dysprothrombinemia: an inherited structural disorder of human prothrombin. J Clin Invest 1969;48:2251-2259
85. Rocha E, Paramo JA, Bascones C, Fisac PR, Cuesta B, Fernandez J. Prothrombin Segovia: a new congenital abnormality of prothrombin. Scand J Haematol 1986;36:444-449
86. Josso F, Monasterio de Sanchez J, Lavergne JM, Menache D, Soulier JP. Congenital abnormality of the prothrombin molecule (factor II) in four siblings: prothrombin Barcelona. Blood 1971;38:9-16
87. Girolami A, Bareggi G, Brunetti A, Sticchi A. Prothrombin Padua: a "new" congenital dysprothrombinemia. J Lab Clin Med 1974;84:654-666
88. Weinger RS, Rudy C, Moake JL, Olson JD, Cimo PL. Prothrombin Houston: a dysprothrombin identifiable by crossed immunoelectrofocusing and abnormal Echis carinatus venom activation. Blood 1980;55:811-816 (Pubitemid 10095989)
89. Smith LG, Coone LA, Kitchens CS. Prothrombin Gainesville. A dysprothrombinemia in a pair of identical twins. Am J Hematol 1981;11:223-231
90. Ruiz-Sáez A, Luengo J, Rodriguez A, Ojeda A, Gómez O, Acurero Z. Prothrombin Perija: a new congenital dysprothrombinemia in an Indian family. Thromb Res 1986;44:587-598
91. Huisse MG, Dreyfus M, Guillin MC. Prothrombin Clamart: prothrombin variant with defective Arg 320-IIe cleavage by factor Xa. Thromb Res 1986;44:11-21
92. Quick AJ, Hussey CV. Hereditary hypoprothrombinaemias. Lancet 1962;1:173-177
93. Josso F, Rio Y, Béguin S. A new variant of human prothrombin: prothrombin Metz, demonstration in a family showing double heterozygosity for congenital hypoprothrombinemia and dysprothrombinemia. Haemostasis 1982;12:309-316 (Pubitemid 13198344)
94. Bezeaud A, Drouet L, Soria C, Guillin MC. Prothrombin Salakta: an abnormal prothrombin characterized by a defect in the active site of thrombin. Thromb Res 1984;34:507-518 (Pubitemid 14111344)
95. Kahn MJ, Govaerts A. Prothrombin Brussels, a new congenital defective protein. Thromb Res 1974;5:141-156
96. Dumont MD, Tapon-Bretaudiere J, Fischer AM, Bros A, Chassevent J, Aufeuvre JP. Prothrombin Poissy: a new variant of human prothrombin. Br J Haematol 1987;66:239-243
97. Rubio R, Almagro D, Cruz A, Corral JF. Prothrombin Habana: a new dysfunctional molecule of human prothrombin associated with a true prothrombin deficiency. Br J Haematol 1983;54:553-560
98. Lutze G, Frick U, Töpfer G, Urbahn H. [Hereditary dysprothrombinemia with a mild bleeding tendency (prothrombin Magdeburg)]. Dtsch Med Wochenschr 1989;114:288-292