The Leu564 Factor XIIIA Variant Results in Significantly Lower Plasma Factor XIII Levels than the Pro564 Variant

Louise Gallivan; Alexander F. Markham; Rashida Anwar

doi:10.1055/s-0037-1614399

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1999; 82(04): 1368-1370
DOI: 10.1055/s-0037-1614399

Letters to the Editor

Schattauer GmbH

The Leu564 Factor XIIIA Variant Results in Significantly Lower Plasma Factor XIII Levels than the Pro564 Variant

Authors

Louise Gallivan

¹Molecular Medicine Unit, University of Leeds, Clinical Sciences Building, St James’s University Hospital, Leeds, UK
Alexander F. Markham

¹Molecular Medicine Unit, University of Leeds, Clinical Sciences Building, St James’s University Hospital, Leeds, UK
Rashida Anwar

¹Molecular Medicine Unit, University of Leeds, Clinical Sciences Building, St James’s University Hospital, Leeds, UK

Abstract

Full Text

References

References
1 Barry ELR, Mosher DF. Factor XIIIa-mediated cross-linking of fibronectin in fibroblast cell-layers: cross-linking of cellular and plasma fibronectin and of amino-terminal fibronectin fragments. J Biol Chem 1989; 264: 4179-85.
2 Sane DC, Moser TL, Pippen AMM, Parker CJ, Achyuthan KE, Greenberg CS. Vitronectin is a substrate for transglutaminases. Biochem Biophys Res Commun 1988; 157: 115-20.
3 Paye M, Nusgens B, Lapiere CM. Factor XIII of blood coagulation decreases the susceptibility of collagen precursors to proteolysis. Biochim Biophys Acta 1991; 1073: 437-41.
4 Borth W, Chang V, Bishop P, Harpel PC. Lipoprotein(a) is a substrate for factor XIIIa and tissue transglutaminase. J Biol Chem 1991; 266: 18149-53.
5 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 1995; 91: 728-35.
6 Suzuki K, Henke J, Iwata M, Henke L, Tsuji H, Fukunaga T, Ishimoto G, Szekelyi M, Ito S. Novel polymorphisms and haplotypes in the human coagulation factor XIIIA subunit gene. Hum Genet 1996; 98: 393-5.
7 Kangsadalampai S, Board PG. The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity. Blood 1998; 92: 2766-70.
8 Kohler HP, Ariens RAS, Whitaker P, Grant PJ. A common coding polymorphism in the FXIII A-subunit gene (FXIIIVal34Leu) affects cross-linking activity. Thromb Haemost 1998; 80: 704.
9 Anwar R, Gallivan L, Edmonds SD, Markham AF. Genotype/phenotype correlations for coagulation factor XIII: specific “normal” polymorphisms are associated with high or low factor XIII specific activity. Blood 1999; 93: 897-905.
10 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 1994; 91: 7296-300.
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 1996; 87: 2769-74.
12 Wisen O, Gardlund B. Hemostasis in Crohn’s disease: Low FXIII levels in active disease. Scand J Gastroent 1988; 23: 961-6.
13 van Wersch JWJ, Peters C, Ubachs JMH. Coagulation factor XIII in plasma of patients with benign and malignant gynaecological tumours. Eur J Clin Chem Clin Biochem 1994; 32: 681-4.
14 Lorenz R, Olbert P, Born P. Factor XIII in chronic inflammatory bowel diseases. Sem Thromb Haemost 1996; 22: 451-5.