Zusammenfassung
Der Blutgerinnungsfaktor XIII (FXIII) spielt eine zentrale Rolle in der Hämostase, da er für die Vernetzung der Fibrinfäden zu einem festen, unlöslichen Gerinnsel verantwortlich ist. Jegliche Gerinnselbildung im menschlichen Körper, sei dies ein Thrombus in einem Koronargefäß (akuter Herzinfarkt) oder ein Embolus in einer Pulmonalarterie (akute Lungenembolie), ist also nur infolge der vernetzenden Funktion von FXIII entstanden. Aus diesem Grund wurde FXIII früher auch “fibrinstabilisierender Faktor„ genannt. Da FXIII nicht wie die anderen Gerinnungsfaktoren zur Gruppe der proteinspaltenden Serinproteasen gehört, sondern Proteine vernetzt, nimmt FXIII schon wegen seiner Funktion eine Sonderstellung unter den Gerinnungsfaktoren ein. Aufgrund dieser zentralen Funktion in der Gerinnselbildung leiden Patienten mit angeborenem, komplettem FXIII-Mangel an einer ausgeprägten und potenziell lebensgefährlichen Blutungsneigung.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
Literatur
Anwar R, Miloszewski KJ (1999) Factor XIII deficiency. Br J Haematol 107: 468–484
Anwar R, Gallivan L, Edmonds SD et al. (1999) Genotype/phenotype correlations for coagulation factor XIII: specific normal polymorphisms are associated with high or low factor XIII specific activity. Blood 93: 897–905
Ariëns RAS, Kohler HP, Mansfield MW et al. (1999) Subunit antigen and activity levels of blood coagulation factor XIII in healthy individuals. Relation to sex, age, smoking, and hypertension. Arterioscler Thromb Vasc Biol 19: 2012–6
Ariëns RAS, Philippou H, Chandrasekaran N et al. (2000) The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure. Blood 96:988–995
Ariëns RAS, Lai TS, Weisel JW et al. (2002) Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms. Blood 100: 743–754
Asahina T, Kobayashi T, Okada Y et al. (2000) Maternal blood coagulation factor XIII is associated with the development of cytotrophoblastic shell. Placenta 21: 388–393
Attié-Castro FA, Zago MA, Lavinha J et al. (2000) Ethnic heterogeneity of the factor XIII Val34Leu polymorphism. Thromb Haemost 84: 601–603
Board PG, Webb GC, McKee J et al. (1988) Localization of the coagulation factor XIII A subunit gene (F13A) to chromosome bands 6p24–p25. Cytogenet Cell Genet 48: 25–27
Board PG, Losowsky MS, Miloszewski KJ (1993) Factor XIII: inherited and acquired deficiency. Blood Rev 7: 229–242
Catto AJ, Kohler HP, Bannen S et al. (1998) Factor XIII gene Val34Leu polymorphism: a novel association with primary intracerebral haemorrhage. Stroke 29: 813–816
Catto AJ, Kohler HP, Coore J et al. (1999) Association of a common polymorphism in the factor XIII gene with venous thrombosis. Blood 93: 906–908
Duckert F, Jung E, Shmerling DH (1960) A hitherto undescribed congenital haemorrhagic diathesis probably due to fibrin stabilizing factor deficiency. Thromb Diath Haemorrh 5: 179–186
Elbaz A, Poirier O, Canaple S et al. (2000) The association between the Val34Leu polymorphism in the factor XIII gene and brain infarction. Blood 95: 586–591
Gemmati D, Serino ML, Ongaro A et al. (2001) A common mutation in the gene for coagulation factor XIII-A (Val34Leu): A risk factor for primary intracerebral hemorrhage is protective against atherothrombotic diseases. Am J Hematol 67: 183–188
Ichinose A (1994) The physiology and biochemistry of factor XIII. In: Bloom AL, Forbes CD, Thomas DP et al. (ed) Haemostasis and Thrombosis, 3rd edn, Vol. 1. Livingstone, Edinburgh pp 531–546
Ichinose A, Asahina T, Kobayashi T (2005) Congenital blood coagulation factor XIII deficiency and perinatal management. Curr Drug Targets 6: 541–549
Inbal A, Muszbek L (2003) Coagulation factor deficiencies and pregnancy loss. Semin Thromb Hemost 29: 171–174
Inbal A, Dardik R (2006) Role of coagulation factor XIII (FXIII) in angiogenesis and tissue repair. Pathophysiol Haemost Thromb 35: 162–165
Ivaskevicius V, Seitz R, Kohler HP et al. (2007) International registry on factor XIII deficiency: a basis formed mostly on European data. Thromb Haemost 97: 914–921
Janus TJ, Lewis SD, Lorand L et al. (1983) Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen. Biochemistry 22: 6269–6272
Kangsadalampai S, Board PG (1998) 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 92: 2766–2770
Katona E, Haramura G, Kárpáti L et al. (2000) A simple, quick one-step ELISA assay for the determination of complex plasma factor XIII (A2B2). Thromb Haemost 83: 268–273
Kohler HP, Ariëns RAS, Whitaker P et al. (1998a) A common coding polymorphism in the factor XIII A-subunit gene (FXIIIVal34Leu) affects cross-linking activity. Thromb Haemost 80: 704
Kohler HP, Stickland MH, Ossei-Gerning N et al. (1998b) Association of a common polymorphism in the factor XIII gene with myocardial infarction. Thromb Haemost 79: 8–13
Kohler HP, Futers TS, Grant PJ (1999) Prevalence of three common polymorphisms in the A-subunit gene of factor XIII in patients with coronary artery disease. Association with FXIII activity and antigen levels. Thromb Haemost 81: 511–515
Lorand L (2001) Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin. Ann N Y Acad Sci 936: 291–311
Lorand L, Graham RM (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4: 140–156
Lorand L (2005) Factor XIII and the clotting of fibrinogen: from basic research to medicine. J Thromb Haemost 3: 1337–1348
Lorenz R, Born P, Olbert P et al. (1995) Factor XIII substitution in ulcerative colitis. Lancet 345: 449–450
Lovejoy AE, Reynolds TC, Visich JE et al. (2006) Safety and pharmacokinetics of recombinant factor XIII-A2 administration in patients with congenital factor XIII deficiency. Blood 108: 57–62
McCormack LJ, Kain K, Catto AJ et al. (1998) Prevalence of FXIIIVal34Leu in populations with different cardiovascular risk. Thromb Haemost 80: 523–524
Meili EO (2002) Krankheitsbild und Behandlung des schweren homozygoten Faktor-XIII-Mangels. Hämostaseologie 22: 48–52
Mikkola H, Syrjälä M, Rasi V et al. (1994) Deficiency in the A-subunit of coagulation factor XIII: two novel point mutations demonstrate different effects on transcript levels. Blood 84: 517–525
Mosesson MW (2005) Fibrinogen and fibrin structure and functions. J Thromb Haemost 3: 1894–1904
Muszbek L, Ádány R, Mikkola H (1996) Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function. Crit Rev Clin Lab Sci 33: 357–421
Noll T, Wozniak G, McCarson K et al. (1999) Effect of factor XIII on endothelial barrier function. J Exp Med 189: 1373–1382
Schroeder V, Meili E, Cung T et al. (2006) Characteristion of six novel Asubunit mutations leading to congenital factor XIII deficiency and molecular analysis of the first diagnosed patient with this rare bleeding disorder. Thromb Haemost 95: 77–84
Schroeder V, Vuissoz JM, Caflisch A et al. (2007) Factor XIII activation peptide is released into plasma upon cleavage by thrombin and shows a different structure compared to its bound form. Thromb Haemost 97: 890–898
Schwartz ML, Pizzo SV, Hill RL et al. (1971) The subunit structures of human plasma and platelet factor XIII (fibrin-stabilizing factor). J Biol Chem 246: 5851–5854
Siebenlist KR, Meh DA, Mosesson MW (1996) Plasma factor XIII binds specifically to fibrinogen molecules containing γ′ chains. Biochemistry 35: 10448–10453
Trumbo TA, Maurer MC (2000) Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation. J Biochem 275: 20627–20631
Visich JE, Zuckerman LA, Butine MD et al. (2005) Safety and pharmacokinetics of recombinant factor XIII in healthy volunteers: a randomized, placebo-controlled, double-blind, multi-dose study. Thromb Haemost 94: 802–807
Vokó Z, Bereczky Z, Katona E et al. (2007) Factor XIIIVal34Leu variant protects against coronary artery disease. A meta-analysis. Thromb Haemost 97: 458–463
Webb GC, Coggan M, Ichinose A et al. (1989) Localization of the coagulation factor XIII B subunit gene (F13B) to chromosome bands 1q31-32.1 and restriction fragment length polymorphism at the locus. Hum Genet 81: 157–160
Weger M, Renner W, Stanger O et al. (2001) Role of factor XIII Val34Leu polymorphism in retinal artery occlusion. Stroke 32: 2759–2761
Wilmer M, Rudin K, Kolde HJ et al. (2001) Evaluation of a sensitive colorimetric FXIII incorporation assay. Effects of FXIII Val34Leu, plasma fibrinogen concentration and congenital FXIII deficiency. Thromb Res 102: 81–91
Wilmer M, Schröder V, Kohler HP (2002) Methoden zur Bestimmung des Faktors XIII/XIIIa. Hämostaseologie 22: 18–28
Yee VC, Pedersen LC, Le Trong I et al. (1994) Three-dimensional structure of a transglutaminase: Human blood coagulation factor XIII. Proc Natl Acad Sci USA 91: 7296–7300
Yee VC, Pedersen LC, Bishop PD et al. (1995) Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res 78: 389–397
Yorifuji H, Anderson K, Lynch GW et al. (1988) B protein of factor XIII: differentiation between free B and complexed B. Blood 72: 1645–1650
Zheng H, Tzeng CC, Butt C et al. (2002) An extremely low prevalence of factor V Leiden, FIIG20210A and FXIIIV34L in Taiwan Chinese population. Thromb Haemost 87: 1081–1082
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2010 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Schroeder, V., Kohler, HP. (2010). Faktor XIII. In: Pötzsch, B., Madlener, K. (eds) Hämostaseologie. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-01544-1_23
Download citation
DOI: https://doi.org/10.1007/978-3-642-01544-1_23
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-01543-4
Online ISBN: 978-3-642-01544-1
eBook Packages: Medicine (German Language)