Characterization of blood coagulation factor XIT4751

Thrombosis and Haemostasis

Volumn 93, Issue 6, 2005, Pages 1082-1088

  McVey, John H ^a   Lal, Kalpana ^a,b   Imanaka, Yasufumi ^a,c   Kemball Cook, Geoffrey ^a   Bolton Maggs, Paula H B ^b   Tuddenham, Edward G D ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b MANCHESTER ROYAL INFIRMARY   (United Kingdom)

^c NARA MEDICAL UNIVERSITY   (Japan)

Author keywords

Deficiency; Factor XI; Glycosylation; Mutation

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; BLOOD CLOTTING FACTOR 11; DNA; ISOLEUCINE; LYSINE; PROLINE; SERINE; SERINE PROTEINASE; THREONINE; RECOMBINANT PROTEIN;

ADOLESCENT; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BLEEDING TENDENCY; BLOOD CLOTTING FACTOR 11 DEFICIENCY; CASE REPORT; CHO CELL; DISEASE SEVERITY; DNA SEQUENCE; ENZYME LINKED IMMUNOSORBENT ASSAY; EXON; GENE EXPRESSION; GENE MUTATION; GENETIC TRANSFECTION; GLYCOSYLATION; HEMATURIA; HUMAN; IMMUNOCYTOCHEMISTRY; IN VITRO STUDY; IN VIVO STUDY; MALE; MUTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; POLYMERASE CHAIN REACTION; PREDICTION; PRIORITY JOURNAL; SINGLE STRAND CONFORMATION POLYMORPHISM; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING; WILD TYPE; AMINO ACID SEQUENCE; ANIMAL; BLOOD; CHEMISTRY; GENETICS; HAMSTER; METABOLISM; MOLECULAR GENETICS; POINT MUTATION; SEQUENCE HOMOLOGY;

ADOLESCENT; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CHO CELLS; CRICETINAE; DNA MUTATIONAL ANALYSIS; FACTOR XI; FACTOR XI DEFICIENCY; HUMANS; MALE; MOLECULAR SEQUENCE DATA; POINT MUTATION; POLYMERASE CHAIN REACTION; POLYMORPHISM, SINGLE-STRANDED CONFORMATIONAL; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFECTION;

EID: 20444466085     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH05-01-0051     Document Type: Article

References (29)

1. Davie EW, Fujikawa K, Kisiel W: The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991; 30: 10363-70.
2. Bouma BN, Griffin JH: Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII. J Biol Chem 1977; 252: 6432-7.
3. Oliver JA, Monroe DM, Roberts HR et al. Thrombin activates factor XI on activated platelets in the absence of factor XII. Arterioscler Thromb Vasc Biol 1999; 19: 170-7.
4. Gailani D, Broze GJJ: Factor XI activation in a revised model of blood coagulation. Science 1991; 253: 909-12.
5. Brunnee T, La Porta C, Reddigari SR et al. Activation of factor XI in plasma is dependent on factor XII [see comments]. Blood 1993; 81: 580-6.
6. Asakai R, Davie EW, Chung DW: Organization of the gene for human factor XI. Biochemistry 1987; 26: 7221-8.
7. Kato A, Asakai R, Davie EW et al. Factor XI gene (F11) is located on the distal end of the long arm of human chromosome 4. Cytogenet Cell Genet 1989; 52: 77-8.
8. Seligsohn U: High gene frequency of factor XI (PTA) deficiency in Ashkenazi Jews. Blood 1978; 51: 1223-8.
9. Asakai R, Chung DW, Ratnoff OD et al. Factor XI (plasma thromboplastin antecedent) deficiency in Ashkenazi Jews is a bleeding disorder that can result from three types of point mutations. Proc Natl Acad Sci U S A 1989; 86: 7667-71.
10. Peretz H, Zivelin A, Usher S et al. A 14-bp deletion (codon 554 del AAGgtaacagagtg) at exon 14/intron N junction of the coagulation factor XI gene disrupts splicing and causes severe factor XI deficiency. Hum Mutat 1996; 8: 77-8.
11. Hancock JF, Wieland K, Pugh RE et al. A molecular genetic study of factor XI deficiency. Blood 1991; 77: 1942-8.
12. O'connell NM, Saunders RE, Lee CA et al. Structural interpretation of 42 mutations causing factor XI deficiency using homology modeling. J Thromb Haemost 2005; 3: 127-38.
13. Meijers JC, Davie EW, Chung DW: Expression of human blood coagulation factor XI: characterization of the defect in factor XI type III deficiency. Blood 1992; 79: 1435-40.
14. Pugh RE, Mcvey JH, Tuddenham EGD et al. Six point mutations that cause factor XI deficiency. Blood 1995; 85: 1509-6.
15. Kunkel LM, Smith KD, Boyer SH et al. Analysis of human Y chromosome-specific reiterated DNA in chromosome variants. Proc Natl Acad Sci U S A 1977; 74: 1245-9.
16. Imanaka Y, Lal K, Nishimura T et al. Identification of two novel mutations in non-Jewish factor XI deficiency. Br J Haematol 1995; 90: 916-20.
17. Hayashi K: PCR-SSCP: A simple and sensitive method for the detection of mutations in genomic DNA. PCR Meth Appl 1991; 1: 34-8.
18. Fujikawa K, Chung DW, Hendrickson LE et al. Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein. Biochemistry 1986; 25: 2417-24.
19. Kemball-Cook G, Garner I, Imanaka Y et al. High-level production of human blood coagulation factors VII and XI using a new mammalian expression vector. Gene 1994; 139: 275-9.
20. Ohkubo Y, O'Brien DP, Kanehiro T et al. Characterization of a panel of monoclonal antibodies to human coagulation factor XI and detection of factor XI in Hep G2 cell conditioned medium. Thromb Haemost 1990; 63: 417-23.
21. Kirkwood TB, Snape TJ: Biometric principles in clotting and clot lysis assays. Clin Lab Haematol 1980; 2: 155-67.
22. Mcmullen BA, Fujikawa K, Davie EW: Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule. Biochemistry 1991; 30: 2050-6.
23. Martincic D, Zimmerman SA, Ware RE et al. Identification of mutations and polymorphisms in the factor XI genes of an African American family by dideoxyfingerprinting. Blood 1998; 92: 3309-17.
24. Helenius A, Aebi M: Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 2004; 73: 1019-49.
25. Guan JL, Machamer CE, Rose JK. Glycosylation allows cell-surface transport of an anchored secretory protein. Cell 1985; 42: 489-96.
26. Larsen GR, Metzger M, Henson K et al. Pharmacokinetic and distribution analysis of variant forms of tissue-type plasminogen activator with prolonged clearance in rat. Blood 1989; 73: 1842-50.
27. Ni H, Blajchman MA, Ananthanarayanan VS et al. Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin. Thromb Res 2000; 99: 407-15.
28. Cousin P, Dechaud H, Grenot C et al. Influence of glycosylation on the clearance of recombinant human sex hormone-binding globulin from rabbit blood. J Steroid Biochem Mol Biol 1999; 70: 115-21.
29. Greer J: Comparative modeling methods: application to the family of the mammalian serine proteases. Proteins 1990; 7: 317-34.