Molecular characterization of factor IX gene mutations in 53 patients with haemophilia B in India

• References

• 1 Jayandharan G, Shaji RV, Chandy M. et al. Identification of factor IX gene defects using a multiplex PCR and CSGE strategy-a first report. J Thromb Haemost 2003; 1: 2051-4.
• 2 Hinks JL, Winship PR, Makris M. et al. A rapid method for haemophilia B mutation detection using conformation sensitive gel electrophoresis. Br J Haematol 1999; 104: 915-8.
• 3 Peake IR, Lillicarp DP, Boulyjenkov V. et al. Haemophilia: strategies for carrier detection and prenatal diagnosis. Bulletin of WHO 1993; 71: 429-58.
• 4 Sutton M, Bouhassira EE, Nagel RL. Polymerase chain reaction amplification applied to the determination of b-like globin cluster haplotypes. Am J Hematol 1989; 32: 66-9.
• 5 Sommer SS, Ketterling RP. The factor IX gene as a model for analysis of human germline mutations: an update. Hum Mol Gen 1996; 5: 1505-14.
• 6 Tartary M, Vidaud D, Piao Y. et al. Detection of a molecular defect in 40 of 44 patients with haemophilia B by PCR and denaturing gradient gel electrophoresis. Br J Haematol 1993; 84: 662-9.
• 7 Montejo JM, Magallon M, Tizzano E. et al. Identification of twenty-one new mutations in the factor IX gene by SSCP analysis. Hum Mutat 1999; 13: 160-5.
• 8 Herbert O, Trossaert M, Boisseau P. et al. Evaluation of denaturing high-performance liquid chromatography (DHPLC) in the screening of mutations in haemophilia B patients. J Thromb Haemost 2004; 2: 2267-9.
• 9 Haemophilia B Mutation database. (Version 13, 2004) http://www.kcl.ac.uk/ip/petergreen/haemBdatabase.html/ A database of point mutations and short additions and deletions in the factor IX gene..
• 10 Jayandharan G, Shaji RV, Nair SC. et al. Novel missense mutations in two patients with factor XI deficiency (Val271Leu and Tyr351Ser) and one patient with combined factor XI and factor IX deficiency (Phe349Val). J Thromb Haemost 2005; 3: 808-11.
• 11 Bottema CDK, Ketterling RP, Li S. et al. Missense mutations and evolutionary conservation of amino acids: evidence that many of the amino acids in factor IX function as “spacer” elements. Am J Hum Genet 1991; 49: 820-38.
• 12 Larson PJ, Stanfield-Oakley SA, VanDusen WJ. et al. Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa is required for its binding to cofactor VIIIa. J Biol Chem 1996; 271: 3869-76.
• 13 Aktimur A, Gabriel MA, Gailani D. et al. The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa. J Biol Chem 2003; 278: 7981-7.
• 14 Enjolras N, Plantier JL, Rodriguez MH. et al. Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion. J Thromb Haemost 2004; 2: 1143-54.
• 15 Bajaj S. Region of factor IXa protease domain that interacts with factor VIIIa: Analysis of select haemophilia B mutants. Thromb Haemost 1999; 82: 218-25.
• 16 Yoshitake S, Schach BG, Foster DC. et al. Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 1985; 24: 3736-50.