New data on FII, FV, FIX and thrombomodulin defects: blood keeps clotting in normal and in peculiar ways

References

• 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
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Bulato C, Radu CM, Campello E, et al. New prothrombin mutation (Arg596Trp, prothrombin Padua 2) associated with venous thromboembolism. Arterioscler Thromb Vasc Biol. 2016;36:1022–1029.
   Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Vincent LM, Tran S, Livaja R, et al. Coagulation factor V(A2440G) causes east Texas bleeding disorder via TFPIα. J Clin Invest. 2013;123:3777–3787.
   Google Scholar
• Cunha ML, Bakhtiari K, Peter J, et al. A novel mutation in the F5 gene (factor V Amsterdam) associated with bleeding independent of factor V procoagulant function. Blood. 2015;125(11):1822–1825.
   Google Scholar
• Langdown J, Luddington RJ, Huntington JA, et al. A hereditary bleeding disorder resulting from a premature stop codon in thrombomodulin (p.Cys537Stop). Blood. 2014;124:1951–1956.
   Google Scholar
• Dargaud Y, Scoazec JY, Wielders SJ, et al. Characterization of an autosomal dominant bleeding disorder caused by a thrombomodulin mutation. Blood. 2015;125:1497–1501. doi: 10.1182/blood-2014-10-604553
   PubMed Web of Science ®Google Scholar
• Esmon CT. The protein C pathway. Chest. 2003;124(Suppl 3):26S–32S. doi: 10.1378/chest.124.3_suppl.26S
   PubMed Web of Science ®Google Scholar
• Dahlbäck B. Pro- and anticoagulant properties of factor V in pathogenesis of thrombosis and bleeding disorders. Int J Lab Hematol. 2016;38 (Suppl 1):4–11. doi: 10.1111/ijlh.12508
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Girolami A, Santarossa C, Cosi E, et al. Bleeding manifestations in heterozygotes with prothrombin deficiency or abnormalities vs. unaffected family members as observed during a long follow-up study. Blood Coagul Fibrinolysis. 2017;28:623–626.
   Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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.
   Google Scholar
• Vincent LM, Tran S, Livaja R, et al. Coagulation factor V (A2440G) causes east Texas bleeding disorder via TFPIα. J Clin Invest. 2013;123:3777–3787.
   Google Scholar
• Girolami A, Ferrari S, Cosi E, et al. Congenital prothrombin defects: they are not only associated with bleeding but also with thrombosis: a new classification is needed. Hematology. 2018;23:105–110. doi: 10.1080/10245332.2017.1359900
   PubMed Web of Science ®Google Scholar
• Henriksen RA, Dunham CK, Miller LD, et al. Prothrombin Greenville, Arg517  Gln, identified in an individual heterozygous for dysprothrombinemia. Blood. 1998;91:2026–2031.
   Google Scholar
• 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.
   Google Scholar
• 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.
   Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Kuang SQ, Hasham S, Phillips MD, et al. Characterization of a novel autosomal dominant bleeding disorder in a large kindred from east Texas. Blood. 2001;97:1549–1554. doi: 10.1182/blood.V97.6.1549
   PubMed Web of Science ®Google Scholar
• Broze GJ Jr, Girard TJ. Factor V, tissue factor pathway inhibitor, and east Texas bleeding disorder. J Clin Invest. 2013;123:3710–3712. doi: 10.1172/JCI71220
   PubMed Web of Science ®Google Scholar
• Dahlbäck B. Pro- and anticoagulant properties of factor V in pathogenesis of thrombosis and bleeding disorders. Int J Lab Hematol. 2016;38(Suppl 1):4–11. doi: 10.1111/ijlh.12508
   PubMed Web of Science ®Google Scholar
• Cunha ML, Bakhtiari K, Peter J, et al. A novel mutation in the F5 gene (factor V Amsterdam) associated with bleeding independent of factor V procoagulant function. Blood. 2015;125:1822–1825.
   Google Scholar
• Wood JP, Ellery PE, Maroney SA, et al. Biology of tissue factor pathway inhibitor. Blood. 2014;123:2934–2943. doi: 10.1182/blood-2013-11-512764
   PubMed Web of Science ®Google Scholar
• Lozier JN. Gene therapy. Factor IX Padua: them that have, give. Blood. 2012:29(120):4452–4453. doi: 10.1182/blood-2012-09-452821
   Web of Science ®Google Scholar
• Cantore A, Nair N, Della Valle P, et al. Hyperfunctional coagulation factor IX improves the efficacy of gene therapy in hemophilic mice. Blood. 2012:29(120):4517–4520.
   Google Scholar
• 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.
   Google Scholar
• 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.
   Google Scholar
• Mazetto Bde M, 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;126:165.
   Google Scholar
• Anastasiou G, Gialeraki A, Merkouri E, et al. Thrombomodulin as a regulator of the anticoagulant pathway: implication in the development of thrombosis. Blood Coagul Fibrinolysis. 2012;23:1–10. doi: 10.1097/MBC.0b013e32834cb271
   PubMed Web of Science ®Google Scholar
• Ohlin AK, Marlar RA. The first mutation identified in the thrombomodulin gene in a 45-year-old man presenting with thromboembolic disease. Blood. 1995;85:330–336.
   PubMed Web of Science ®Google Scholar
• Girolami A, Fabris F, Dal Bo Zanon R, et al. Factor VII Padua: a congenital coagulation disorder due to an abnormal factor VII with a peculiar activation pattern. J Lab Clin Med. 1978;91:387–395.
   PubMed Web of Science ®Google Scholar
• Girolami A, Molaro G, Lazzarin M, et al. A ‘new’ congenital haemorrhagic condition due to the presence of an abnormal factor X (factor X friuli): study of a large kindred. Br J Haematol. 1970 Aug;19:179–192. doi: 10.1111/j.1365-2141.1970.tb01615.x
   PubMed Web of Science ®Google Scholar