Insight into molecular changes of the FIX protein in a series of Italian patients with haemophilia B

Haemophilia

Volumn 12, Issue 3, 2006, Pages 263-270

  Bicocchi, M P ^a   Pasino, Mirrela ^a   Rosano, C ^b   Molinari, A C ^a   Della Valle, E ^a   Lanza, T ^a   Bottini, F ^a   Acquila, M ^a  

^a G GASLINI INSTITUTE   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

Author keywords

F9 gene; FIX protein; Haemophilia B; Homology modelling; Missense mutation; Structural effects

Indexed keywords

BLOOD CLOTTING FACTOR 9;

ARTICLE; CLINICAL ARTICLE; GENE INDUCTION; GENE MUTATION; GENE SEQUENCE; GENETIC TRANSCRIPTION; HEMOPHILIA B; HUMAN; ITALY; MISSENSE MUTATION; MOLECULAR MODEL; PATHOPHYSIOLOGY; PREDICTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; AMINO ACIDS; ANIMALS; DNA MUTATIONAL ANALYSIS; EXONS; FACTOR IX; HEMOPHILIA B; HUMANS; MODELS, GENETIC; MUTATION, MISSENSE;

EID: 33645961280     PISSN: 13518216     EISSN: 13652516     Source Type: Journal    
DOI: 10.1111/j.1365-2516.2006.01275.x     Document Type: Article

References (32)

1. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K. Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 1985; 24: 3736-50.
2. Di Scipio RG, Kurachi K, Davie EW. Activation of human factor IX (Christmas factor). J Clin Invest 1978; 61: 1528-38.
3. Giannelli F, Green PM, Sommer SS et al. Haemophilia B: Database of point mutations and short additions and deletions-eighth edition. Nucleic Acids Res 1998; 26: 265-8.
4. Bicocchi MP, Pasino M, Bottini F, Lanza T, Mori PG, Acquila M. Mutation analysis is an essential strategy in the genetic counselling of sporadic haemophilia B families. Haemophilia 2002; 8: 730-2.
5. Hinks JL, Winship PR, Makris M, Preston FE, Peake IR, Goodeve AC. A rapid method for haemophilia B mutation detection using conformation sensitive gel electrophoresis. Br J Haematol 1999;104: 915-8.
6. Brandstetter H, Bauer M, Huber R, Lollar P, Bode W. X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B. Proc Natl Acad Sci U S A 1995; 92: 9796-800.
7. Hopfner KP, Lang A, Karcher A et al. Coagulation factor IXa: The relaxed conformation of Tyr99 blocks substrate binding. Struct Fold Des 1999; 7: 989-96.
8. Weiner SJ, Kollman PA, Case DA et al. A new force field for the molecular mechanical simulation of nucleic acids and proteins. J Am Chem Soc 1984; 106: 765-84.
9. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997; 53: 240-55.
10. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993; 26: 283-91.
11. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991; 47: 110-9.
12. Chen SW, Pellequer JL, Schved JF, Giansily-Blaizot M. Model of a ternary complex between activated factor VII, tissue factor and factor IX. Thromb Haemost 2002; 88: 74-82.
13. Tavassoli K, Eigel A, Wilke K, Pollmann H, Horst J. Molecular diagnostics of 15 hemophilia A patients: Characterization of eight novel mutations in the factor VIII gene, two of which result in exon skipping. Hum Mutat 1998; 12: 301-3.
14. Cartegni L, Chew SL, Krainer AR. Listening to silence and understanding nonsense: Exonic mutations that affect splicing. Nat Rev Genet 2002; 3: 285-98.
15. Wang J, Smith PJ, Krainer AR, Zhang MQ. Distribution of SR protein exonic splicing enhancer motifs in human protein-coding genes. Nucleic Acids Res 2005; 33: 5053-62.
16. Green PM, Rowley G, Giannelli F. Unusual expression of the F9 gene in peripheral lymphocytes hinders investigation of F9 mRNA in hemophilia B patients. J Thromb Haemost 2003; 1: 2675-6.
17. Cutler JA, Mitchell MJ, Savidge GF. More on: Unusual expression of the F9 gene in peripheral lymphocytes hinders investigation of F9 mRNA in hemophilia B patients. J Thromb Haemost 2004; 2: 1021.
18. Van de Water NS, Tan T, May S, Browett PJ, Harper P. Factor IX polypyrimidine tract mutation analysis using mRNA from peripheral blood leukocytes. J Thromb Haemost 2004; 2: 2073-5.
19. Roberts HR. Molecular biology of hemophilia B. Thromb Haemost 1993; 70: 1-9.
20. Nelsestuen GL, Resnick RM, Wei GJ, Pletcher CH, Bloomfield VA. Metal ion interactions with bovine prothrombin and prothrombin fragment: 1. Stoichiometry of binding, protein self-association, and conformational change induced by a variety of metal ions. Biochemistry 1981; 20: 351-8.
21. Sperling R, Furie BC, Blumenstein M, Keyt B, Furie B. Metal binding properties of gamma-carboxyglutamic acid. Implications for the vitamin K-dependent blood coagulation proteins. J Biol Chem 1978; 253: 3898-906.
22. Bentley AK, Rees DJ, Rizza C, Brownlee GG. Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position-4. Cell 1986; 45: 343-8.
23. Galeffi P, Brownlee GG. The propeptide region of clotting factor IX is a signal for a vitamin K dependent carboxylase: Evidence from protein engineering of amino acid -4. Nucleic Acids Res 1987; 15: 9505-13.
24. Bristol JA, Furie BC, Furie B. Propeptide processing during factor IX biosynthesis. Effect of point mutations adjacent to the propeptide cleavage site. J Biol Chem 1993; 268: 7577-84.
25. Ware J, Diuguid DL, Liebman HA et al. Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties. J Biol Chem 1989; 264: 11401-6.
26. Gilbert GE, Arena AA. Activation of the factor VIIIa-factor IXa enzyme complex of blood coagulation by membranes containing phosphatidyl-L-serine. J Biol Chem 1996; 271: 11120-5.
27. Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem 1996; 271: 16227-36.
28. Grant MA, Baikeev RF, Gilbert GE, Rigby AC. Lysine 5 and phenylalanine 9 of the factor IX omega-loop interact with phosphatidylserine in a membrane-mimetic environment. Biochemistry 2004; 43: 15367-78.
29. Melton LG, Li T, Stafford DW, Gabriel DA. Location of the platelet binding site in zymogen coagulation factor IX. Blood Coagul Fibrinolysis 2001; 12: 237-43.
30. Noyes CM, Griffith MJ, Roberts HR, Lundblad RL. Identification of the molecular defect in factor IX Chapel Hill: Substitution of histidine for arginine at position 145. Proc Natl Acad Sci U S A 1983; 80: 4200-2.
31. Colman RW, Bradford HN, Kunapuli SP et al. Leu271-Glu292 in kininogens blocks thrombin-induced aggregation. Immunopharmacology 1996; 32: 80-1.
32. Miyata T, Sakai T, Sugimoto M et al. Factor IX Amagasaki: A new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities. Biochemistry 1991; 30: 11286-91.