Molecular characterization of coagulation factor XII deficiency in a Japanese family

Thrombosis and Haemostasis

Volumn 90, Issue 1, 2003, Pages 59-63

  Wada, Hideo ^a   Nishioka, Junji ^b   Kasai, Yasunari ^b   Kato Nakazawa, Keiko ^b   Abe, Yasunori ^b   Morishita, Yoshitaka ^b   Nakatani, Kaname ^a   Nobori, Tsutomu ^a  

^a MIE UNIVERSITY   (Japan)

^b MIE UNIVERSITY HOSPITAL   (Japan)

Author keywords

Coagulation factor XII; Protein folding; W486C mutation

Indexed keywords

ANTIGEN; ANTITHROMBIN; BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 12; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9; COMPLEMENTARY DNA; HIGH MOLECULAR WEIGHT KININOGEN; MUTANT PROTEIN; PLASMINOGEN; PROTEIN C; PROTEIN S; PROTEINASE;

ANTIGEN FUNCTION; ARTICLE; BLOOD CLOTTING FACTOR 12 DEFICIENCY; CATALYSIS; CELL LYSATE; CULTURE MEDIUM; FAMILY; FEMALE; FIBRINOLYSIS; GENE EXPRESSION; GENE IDENTIFICATION; GENE MUTATION; GENE SEQUENCE; GENETIC ANALYSIS; GENETIC POLYMORPHISM; HOMOZYGOSITY; HUMAN; HUMAN CELL; JAPAN; MALE; MOLECULAR BIOLOGY; NUCLEOTIDE SEQUENCE; PLASMID; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; SEQUENCE ANALYSIS; WILD TYPE;

EID: 0037623684     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613599     Document Type: Article

References (26)

1. Ratnoff OD, Colopy JE. Familial hemorrhagic trait associated with deficiency of clot-promoting fraction of plasma. J Clin Invest 1955; 34: 602-13.
2. Griffin JH, Cochrane CG. Human factor XII (Hageman factor). Methods Enzymol 1976; 45: 56-65.
3. Fujikawa K, Davie EW. Human factor XII (Hagman factor). Methods Enzymol 1981; 80: 198-211.
4. Tans G, Rosing J. Structural and functional characterization of factor XII. Semin Thromb Haemost 1987; 13: 1-14.
5. Haanen C, Hommes F, Benraad H, Morselt G. A case of Hageman factor deficiency and a method to purify the factor. Thromb Diath Haemorrh 1960; 5: 201-7.
6. Didisheim P. Hageman factor deficiency (Hageman trait). Arch Intern Med 1962; 110: 74-81.
7. Ikkala E, Myllylä G, Nevanlinna HR. Rare congenital coagulation factor defects in Finland. Scand J Haematol 1971; 8: 210-5.
8. Glucck HI, Rochill W. Myocardial infarction in a patient with a Hageman (factor XII) defect. Ann Intern Med 1966; 64: 390-6.
9. McPherson RA. Thromboembolism in Hageman trait. Am J Clin Pathol 1977; 68: 420-3.
10. Hellstern P, Köhler M, Schmengler K, Doenecke P, Wenzel E. Arterial and venous thrombosis and normal response to streptokinase treatment in a young patient with severe Hageman factor deficiency. Acta Haematol 1983; 69: 123-6.
11. Lodi S, Isa L, Pollini E, Ferrari BA, Scalvini A. Defective intrinsic fibrinolytic activity in a patient with severe factor XII deficiency and myocardial infarction. Scand J Haematol 1984; 33: 80-82.
12. Royle NJ, Nigli M, Cool D, MacGillivray RT, Hamerton JL. Structure gene encoding human FXII is located at 5q33-qter. Somatic Cell Molec Genet 1988; 14: 217-21.
13. Cool DE, Edgell CJ, Louie GV, Zoller MJ, Brayer GD, MacGillivray RT: Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-FXIIa. J Biol Chem 1985; 260: 13666-76.
14. Tripodi M, Citarella F, Guida S, Galeffi P, Fanotoni A, Cortese R. cDNA sequence coding for human coagulation factor XII (Hageman). Nucleic Acids Res 1986; 13: 3146.
15. Cool DE, MacGillivray RT. Characterization of human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5′-prime flanking region. J Biol Chem 1987; 262: 13662-73.
16. Bernadi F, Marchetti G, Patracchini P, et al. Factor XII gene alteration in Hageman trait detected by Taq I restriction enzyme. Blood 1987; 69: 1421-4.
17. Hofferbert S, Müller J, Köstering H, Von Ohlen WD, Schloesser M. A novel 5′ upstream mutation in the factor XII gene associated with Taq I restriction site in an Alu repeat in factor XII deficient patient. Hum Genet 1996; 97: 838-41.
18. Miyata T, Kawabata S, Iwanaga S, Takahashi I, Alving B, Saito H. Coagulation factor XII (Hageman factor) Washington D.C.: Inactive factor XIIa results from Cys-571→Ser substitution. Proc Natl Acad Sci USA 1989; 86: 8319-22.
19. Hovinga JK, Schaller J, Stricker H, et al. Coagulation factor XII Locarno: The function defect is caused by the amino acid substitution Arg 353→Pro leading to loss of a kallikerin cleavage site. Blood 1994; 84: 1173-81.
20. Schlosser M, Zeerleder S, Lutze G, et al. Mutations in the human factor XII gene. Blood 1997; 90: 3967-77.
21. Kanaji T, Okamura T, Kamura T, Niho Y, Sugiyama M. Molecular analysis of a family with factor XII deficiency. Identification of 126 Arg to Pro substitution. Blood 1995; 86: 876a.
22. Kanaji T, Okamura T, Osaki K, et al. A common genetic polymorphism (46C to T substitution) in the 5′-untranslated region to coagulation factor XII gene is associated with low translation efficiency and decrease in plasma factor XII level. Blood 1998; 91: 2010-4.
23. Kondo S, Tokunaga F, Kuwano S, Oono Y, Kumagai S, Koide T. Factor XII Tenri, a novel cross reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation. Blood 1999; 93: 4300-8.
24. Kanaji T, Kanaji S, Osaki K, et al. Identification and characterization of two novel mutations (Q421 and R123 P) in congenital factor XII deficiency. Thromb Haemost 2001, 86; 1409-15.
25. Kopito PR. ER quality control: The cytoplasmic connection. Cell 1997; 88: 427-30.
26. Kim PS, Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: Disorders of protein trafficking and the role of ER molecular chaperones. Endocrine Rev 1998; 19: 173-202.