Molecular mechanisms of Type II factor XIII deficiency: Novel Gly562- Arg mutation and C-terminal truncation of the A subunit cause factor XIII deficiency as characterized in a mammalian expression system

Blood

Volumn 91, Issue 8, 1998, Pages 2830-2838

  Takahashi, Nobumasa ^b   Tsukamoto, Hiroaki ^b   Umeyama, Hideaki ^b   Castaman, Giancarlo ^b   Rodeghiero, Francesco ^b   Ichinose, Akitada ^a  

^a YAMAGATA UNIVERSITY   (Japan)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BLOOD CLOTTING FACTOR 13 DEFICIENCY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; GENE AMPLIFICATION; GENE EXPRESSION; HUMAN; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SOUTHERN BLOTTING;

EID: 0032523163     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v91.8.2830.2830_2830_2838     Document Type: Article

References (40)

1. Folk JE, Chung SI: Blood coagulation factor XIII: Relationship of some biological properties to subunit structure, in Reich E, Rifkin DB, Shaw E (eds): Proteases and Biological Control. New York, NY, Cold Spring Harbor Laboratory, 1975, p 157
2. Lorand L, Losowsky MS, Miloszewski KJM: Human factor XIII. Fibrin-stabilizing factor. Prog Thromb Hemost 5:245, 1980
3. Ichinose A: Physiology and biochemistry of factor XIII, in Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD (eds): Haemostasis and Thrombosis. Edinburgh, UK, Churchill Livingstone, 1995, p 531
4. Ichinose A, McMullen BA, Fujikawa K, Davie EW: Amino acid sequence of the B subunit of human factor XIII, a protein composed of ten repetitive segments. Biochemistry 25:4633, 1986
5. Ichinose A, Hendrickson LE, Fujikawa K, Davie EW: Amino acid sequence of the A subunit of human factor XIII. Biochemistry 25:6900, 1986
6. Ichinose A, Bottenus RE, Davie EW: Structure of transglutaminases. J Biol Chem 265:13411, 1990
7. Ichinose A, Davie EW: Characterization of the gene for the A subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci USA 85:5829, 1988
8. Bottenus RE, Ichinose A, Davie EW: Nucleotide sequence of the gene for the B subunit of human factor XIII. Biochemistry 29:11195, 1990
9. Ichinose A, Kaetsu H: Molecular approach to the structure-function relationship of human coagulation factor XIII. Method Enzymol 222:36, 1993
10. Girolami A, Burul A, Fabris F, Cappellato G, Betterle C: Studies on factor XIII antigen in congenital factor XIII deficiency. A tentative classification of the disease in two groups. Folia Haematol 105:131, 1978
11. Izumi T, Hashiguchi T, Castaman G, Tosetto A, Rodeghiero F, Girolami A, Ichinose A: Type I factor XIII deficiency is caused by a genetic defect of its B subunit: Insertion of triplet AAC in exon III leads to premature termination in the second Sushi domain. Blood 87:2769, 1996
12. Hashiguchi T, Saito M, Morishita E, Matsuda T, Ichinose A: Two genetic defects in a patient with complete deficiency of the B subunit for factor XIII. Blood 82:145, 1993
13. Hashiguchi T, Ichinose A: Molecular and cellular basis of deficiency of the B subunit for factor XIII secondary to a Cys430-Phe mutation in the seventh Sushi domain. J Clin Invest 95:1002, 1995
14. Ichinose A, Izumi T, Hashiguchi T: The normal and abnormal genes of the A and B subunits in coagulation factor XIII. Semin Thromb Haemost 22:385, 1996
15. Kamura T, Okamura T, Murakawa M, Tsuda H, Teshima T, Shibuya T, Harada M, Niho Y: Deficiency of coagulation factor XIII A subunit caused by the dinucleotide deletion at the 5′ end of exon III. J Clin Invest 90:315, 1992
16. Board P, Coggan M, Miloszewski K: Identification of a point mutation in factor XIII A subunit deficiency. Blood 80:937, 1992
17. 171-stop codon) in factor XIII A subunit deficiency. Br J Haematol 85:769, 1993
18. Mikkola H, Syrjala M, Rasi V, Vahtere E, Hamalainen E, Peltonen L, Palotie A: Deficiency in the A-subunit of coagulation factor XIII: Two novel point mutations demonstrate different effects on transcript levels. Blood 84:517, 1994
19. A subunit. Br J Haematol 91:452, 1995
20. Anwar R, Stewart AD, Miloszewski KJA, Losowsky MS, Markham AF: Molecular basis of inherited factor XIII deficiency: Identification of multiple mutations provides insights into protein function. Br J Haematol 91:728, 1995
21. Vreken P, Niessen RWLM, Peters M, Schaap MCL, Zuithoff-Rijntijes JGM, Sturk A: A point mutation in an invariant splice acceptor site results in a decreased mRNA level in a patient with severe coagulation factor XIII subunit A deficiency. Thromb Haemost 74:584, 1995
22. Mikkola H, Yee VC, Syrjala M, Seitz R, Egbring R, Petrini P, Ljung R, Ingerslev J, Teller DC, Peltonen L, Palotie A: Four novel mutations in deficiency of coagulation factor XIII: Consequence of expression and structure of the A-subunit. Blood 87:141, 1996
23. Kangsadalampai S, Forges-Berth A, Caglayan SH, Board PG: New mutations causing the premature termination of translation in the A subunit gene of coagulation factor XIII. Thromb Haemost 76:139, 1996
24. Coggan M, Baker R, Miloszewski K, Woodfield G, Board P: Mutations causing coagulation factor XIII subunit A deficiency: Characterization of the mutant proteins after expression in yeast Blood 85:2455, 1995
25. A subunit deficiency due to a homozygous 13-base pair deletion in exon 3 of the A subunit gene. Am J Hematol 53:77, 1996
26. Mikkola H, Muszbek L, Laiho E, Syrjala M, Hamalainen E, Haramura G, Salmi T, Peltonen L, Plotie A: Molecular mechanism of a mild phenotype in coagulation factor XIII (FXIII) deficiency: A splicing mutation permitting partial correct splicing of FXIII A-subunit mRNA. Blood 89:1279, 1997
27. Kaetsu H, Hashiguchi T, Foster D, Ichinose A: Expression of the A and B subunits for human coagulation factor XIII in baby hamster kidney (BHK) cells: Release of the recombinant A subunit of factor XIII independent of the classical secretory pathway. J Biochem 119:961, 1996
28. Rodeghiero F, Tosetto A, Di Bona E, Castaman G: Clinical pharmacokinetics of a placenta-derived factor XIII concentrate in type I and type II factor XIII deficiency. Am J Hematol 36:30, 1991
29. Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain-termination inhibitors. Proc Natl Acad Sci USA 74:5463, 1977
30. Yee VC, Pedersen LC, Trong IL, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: Human blood coagulation factor XIII. Proc Natl Acad Sci USA 91:7296, 1994
31. Kurochkin IV, Procyk R, Bishop PD, Yee VC, Teller DC, Ingham KC, Medved LV: Domain structure, stability and domain-domain interactions in recombinant factor XIII. J Mol Biol 248:414, 1995
32. Yoneda T, Komooka H, Umeyama H: A computer modeling study of the interaction between tissue factor pathway inhibitor and blood coagulation factor Xa. J Protein Chem 16:597, 1997
33. Yoneda S, Umeyama H: Free energy perturbation calculations on multiple mutation basis. J Chem Phys 97:6730, 1992
34. Weiner SJ, Kollman PA, Case DA, Singh UC, Ghio C, Alagona G, Profeta S, Weiner P: A new force field for molecular mechanical simulation of nucleic acids and proteins. J Am Chem Soc 106:765, 1984
35. Du Z, Regier DA, Desrosiers RC: Improved recombinant PCR mutagenesis procedure that uses alkaline-denatured plasmid template. Biotechniques 18:376, 1995
36. Cooper DN: Human gene mutations affecting RNA processing and translation. Ann Med 25:11, 1993
37. Tokunaga F, Muta T, Iwanaga S, Ichinose A, Davie EW, Kuma K, Miyata T: Limulus hemocyte transglutaminase: cDNA cloning, amino acid sequence, and tissue localization. J Biol Chem 268:262, 1993
38. Grant FJ, Tayler DA, Sheppard PO, Mathewes SL, Lint W, Vanaja E, Bishop PD, O'Hara PJ: Molecular cloning and characterization of a novel transglutaminase cDNA from a human prostate cDNA library. Biochem Biophys Res Commun 203:1117, 1994
39. Lai T-S, Achyuthan KE, Santiago MA, Greenberg CS: Carboxylterminal truncation of recombinant factor XIII A-chains. J Biol Chem 269:24596, 1994
40. Mikkola, Muzbek L, Haramura G, Hamalainen E, Jalanko A, Palotie A: Molecular mechanisms oif mutations in factor XIIIA-subunit deficiency: In vitro expression in cos-cells demonstrates intracellular degeneration of the mutant proteins. Thromb Haemost 77:1068, 1997