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Hemostasis and Thrombosis

Congenital prothrombin defects: they are not only associated with bleeding but also with thrombosis: a new classification is needed

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References

  • Girolami A, Scarano L, Saggiorato G, et al. Congenital deficiencies and abnormalities of prothrombin. Blood Coagul Fibrinolysis. 1998;9:557–569. doi: 10.1097/00001721-199810000-00001
  • Lancellotti S, De Cristofaro R. Congenital prothrombin deficiency. Semin Thromb Hemost. 2009;35:367–381. doi: 10.1055/s-0029-1225759
  • Lancellotti S, Basso M, De Cristofaro R. Congenital prothrombin deficiency: an update. Semin Thromb Hemost. 2013;39:596–606. doi: 10.1055/s-0033-1348948
  • Lefkowitz JB, Weller A, Nuss R, et al. A common mutation, Arg457-->Gln, links prothrombin deficiencies in the Puerto Rican population. J Thromb Haemost. 2003;1:2381–2388. doi: 10.1046/j.1538-7836.2003.00420.x
  • Girolami A, Scandellari R, Scapin M, et al. Congenital bleeding disorders of the vitamin K-dependent clotting factors. Vitam Horm. 2008;78:281–374. doi: 10.1016/S0083-6729(07)00014-3
  • Miyawaki Y, Suzuki A, Fujita J, et al. Thrombosis from a prothrombin mutation conveying antithrombin resistance. N Engl J Med. 2012;366:2390–2396. doi: 10.1056/NEJMoa1201994
  • Sivasundar S, Oommen AT, Prakash O, et al. Molecular defect of ‘Prothrombin Amrita’: substitution of arginine by glutamine (Arg553 to Gln) near the Na(+) binding loop of prothrombin. Blood Cells Mol Dis. 2013;50:182–183. doi: 10.1016/j.bcmd.2012.11.008
  • Djordjevic V, Kovac M, Miljic P, et al. A novel prothrombin mutation in two families with prominent thrombophilia – the first cases of antithrombin resistance in a Caucasian population. J Thromb Haemost. 2013;11:1936–1939.
  • Kishimoto M, Suzuki N, Murata M, et al. The first case of antithrombin-resistant prothrombin Belgrade mutation in Japanese. Ann Hematol. 2016;95:541–542. doi: 10.1007/s00277-015-2533-6
  • Bulato C, Radu CM, Campello E, et al. New prothrombin mutation (Arg596Trp, prothrombin Padua 2) associated with venous thromboembolism significance. Arterioscler Thromb Vasc Biol. 2016;36:1022–1029. doi: 10.1161/ATVBAHA.115.306914
  • Akhavan S, De Cristofaro R, Peyvandi F, et al. 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. doi: 10.1182/blood-2002-01-0243
  • Henriksen RA, Dunham CK, Miller LD, et al. Prothrombin Greenville, Arg517→Gln, identified in an individual heterozygous for dysprothrombinemia. Blood. 1998;91:2026–2031.
  • Henriksen RA, Owen WG, Nesheim ME, et al. Identification of a congenital dysthrombin, thrombin quick. J Clin Invest. 1980;66:934–940. doi: 10.1172/JCI109961
  • Miyata T, Aruya R, Umeyama H, et al. Prothrombin Salakta: substitution of glutamic acid 466 by alanina residues the fibrinogen clotting activity and the esterase activity. Biochem. 1992;31:7457–7462. doi: 10.1021/bi00148a005
  • 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.
  • 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.
  • Stanchev H, Philips M, Villoutreix BO, et al. 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.
  • Ding Q, Yang L, Zhao X, et al. Paradoxical bleeding and thrombotic episodes of dysprothrombinaemia due to a homozygous Arg382His mutation. Thromb Haemost. 2017;117:479–490. doi: 10.1160/TH16-10-0750
  • Lusher JH. Thrombogenicity associated with factor IX complex concentrates. Semin Hematol. 1991;28:3–5.
  • Girolami A, Tezza F, Scandellari R, et al. Associated prothrombotic conditions are probably responsible for the occurrence of thrombosis in almost all patients with congenital FVII deficiency. critical review of the literature. J Thromb Thrombolysis. 2010;30:172–178. doi: 10.1007/s11239-009-0435-y
  • Girolami A, Ruzzon E, Fabris F, et al. Myocardial infarction and other arterial occlusions in hemophilia a patients. A cardiological evaluation of all 42 cases reported in the literature. Acta Haematol. 2006;116:120–125. doi: 10.1159/000093642
  • Girolami A, Cosi E, Tasinato V, et al. Pulmonary embolism in congenital bleeding disorders: intriguing discrepancies among different clotting factors deficiencies. Blood Coagul Fibrinolysis. 2016;27:517–525. doi: 10.1097/MBC.0000000000000437
  • Girolami A, Bertozzi I, Rigoni I, et al. Congenital FVII deficiency and thrombotic events after replacement therapy. J Thromb Thrombolysis. 2011;32:362–367. doi: 10.1007/s11239-011-0603-8
  • Poort SR, Njo KT, Vos HL, et al. Two novel mutations in the prothrombin gene cause severe bleeding in a compound heterozygous patient. Blood Coagul Fibrinolysis. 1998;9:761–764. doi: 10.1097/00001721-199811000-00007
  • 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.
  • 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.
  • Girolami A, Candeo N, Vettore S, et al. The clinical significance of the lack of arterial or venous thrombosis in patients with congenital prothrombin or FX deficiency. J Thromb Thrombolysis. 2010;29:299–302. doi: 10.1007/s11239-009-0342-2
  • Simioni P, Tormene D, Tognin G, et al. X-linked thrombophilia with a mutant factor IX (factor IX Padua). N Engl J Med. 2009;361:1671–1675. doi: 10.1056/NEJMoa0904377
  • De Moraes Mazetto B, Orsi FL, Siqueira LH, et al. Prevalence of factor IX-R338L (factor IX Padua) in a cohort of patients with venous thromboembolism and mild elevation of factor IX levels. Thromb Res. 2010;126:e165. doi: 10.1016/j.thromres.2010.04.019
  • Koenderman JS, Bertina RM, Reitsma PH, et al. Factor IX-R338L (factor IX Padua) screening in a Dutch population of sibpairs with early onset venous thromboembolism. Thromb Res. 2011;128:603. doi: 10.1016/j.thromres.2011.07.009
  • Monahan PE, Sun J, Gui T, et al. Employing a gain-of-function factor IX variant R338L to advance the efficacy and safety of hemophilia B human gene therapy: preclinical evaluation supporting an ongoing adeno-associated virus clinical trial. Hum Gene Ther. 2015;26:69–81. doi: 10.1089/hum.2014.106
  • Cantore A, Nair N, Della Valle P, et al. Hyperfunctional coagulation factor IX improves the efficacy of gene therapy in hemophilic mice. Blood. 2012;120(23):4517–4520. doi: 10.1182/blood-2012-05-432591

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