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DOI: 10.1055/s-0037-1622010
FXIII und endotheliale Barrierenfunktion
Factor XIII and endothelial barrier functionPublikationsverlauf
Publikationsdatum:
29. Dezember 2017 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00034925/200201/lookinside/thumbnails/10-1055-s-0037-1622010_de-1.jpg)
Zusammenfassung
Die Plasmatransglutaminase FXIIIa (FXIIIa) vernetzt Fibrinmonomere zu einem stabilen Thrombus. Aufgrund dieser Eigenschaft spielt der FXIIIa eine bedeutende Rolle bei der Blutgerinnung und Fibrinolyse. Darüber hinaus ist bereits lange bekannt, dass FXIIIa auch an Zelladhäsion und Migration, Aufbau der extrazellulären Matrix, Gewebereparatur und Wundheilung beteiligt ist. Neue experimentelle Befunde zeigen, dass FXIIIa die endotheliale Schranke stabilisieren kann. Dabei reduziert FXIIIa die Makromolekülpermeabilität in kultivierten Endothelzellschichten und verhindert ein drohendes Schrankenversagen (z. B. während Ischämie-Reperfusion) im Koronarsystem des isolierten Herzens. Diese Wirkung auf die endotheliale Schrankenfunktion wird der Eigenschaft des FXIIIa zugeschrieben, eine Reihe von Proteinen zu vernetzen, die in der extrazellulären Matrix im Bereich der interendothelialen Spalten vorkommen.
Summary
Activated factor XIII (FXIIIa) crosslinks fibrin monomers to a stable clot. Due to this function, FXIIIa plays a major role in hemostasis and fibrinolysis. Additionally, it is well known that FXIIIa has a special meaning in cell adhesion and migration, in generation of extracellular matrix, in tissue repair and wound healing. New experimental studies revealed a FXIIIa stabilizing endothelial barrier function. In this function, FXIIIa reduces endothelial permeability for macromolecules in cultured endothelial monolayers and prevents impending barrier failure in coronary arteries of isolated hearts. This effect is due to the cross-linking of several proteins within the extracellular matrix, especially in the interendothelial clefts.
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Literatur
- 1 Barry EL, Mosher DF. Factor XIII cross-linking of fibronectin at cellular matrix assembly sites. J Biol Chem 1988; 263: 10464-9.
- 2 Fukui H, Kamitsuji H, Nagao T, Yamada K, Akatsuka J, Inagaki M, Shike S, Kobayashi Y, Yoshioka K, Maki S. et al Clinical evaluation of a pasteurized factor XIII concentrate administration in Henoch-Schoenlein purpura. Japanese Pediatric Group. Thromb Res 1989; 56: 667-75.
- 3 Hirahara K, Shinbo K, Takahashi M, Matsuishi T. Suppressive effect of human blood coagulation factor XIII on the vascular permeability induced by anti-guinea pig endothelial cell anti-serum in guinea pigs. Thromb Res 1993; 71: 139-48.
- 4 Kamitsuji H, Tani K, Yasui M, Taniguchi A, Taira K, Tsukada S, Iida Y, Kanki H, Fukui H. Activity of blood coagulation factor XIII as a prognostic indicator in patients with Henoch-Schoenlein purpura. Efficacy of factor XIII substitution. Eur J Pediatr 1987; 146: 519-23.
- 5 Knox P, Crooks S, Rimmer CS. Role of fibronectin in the migration of fibroblasts into plasma clots. J Cell Biol 1986; 102: 2318-23.
- 6 Lorenz R, Born P, Olbert P, Classen M. Factor XIII substitution in ulcerative colitis. Lancet 1995; 345: 449-50.
- 7 Lorand L, Losowsky MS, Miloszewski KJ. Human factor XIII: fibrin-stabilizing factor. Prog Hemost Thromb 1980; 5: 245-90.
- 8 Michel CC, Curry FR. Microvascular permeability. Physiol Rev 1999; 79: 703-61.
- 9 Muhs A, Noll T, Piper HM. Vinculin phosphorylation and barrier failure of coronary endothelial monolayers under energy depletion. Am J Physiol 1997; 273: H608-H617.
- 10 Muszbek L, Adany R, Mikkola H. Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function. Crit Rev Clin Lab Sci 1996; 33: 357-421.
- 11 Noll T, Muhs A, Besselmann M, Watanabe H, Piper HM. Initiation of hyperpermeability in energy-depleted coronary endothelial monolayers. Am J Physiol 1995; 268: H1462-70.
- 12 Noll T, Wozniak G, McCarson K, Hajimohammad A, Metzner HJ, Inserte J, Kummer W, Hehrlein FW, Piper HM. Effect of factor XIII on endothelial barrier function. J Exp Med 1999; 189: 1373-82.
- 13 Sane DC, Moser TL, Pippen AM, Parker CJ, Achyuthan KE, Greenberg CS. Vitronectin is a substrate for transglutaminases. Biochem Biophys Res Commun 1988; 157: 115-20.
- 14 Ueki S, Takagi J, Saito Y. Dual functions of transglutaminase in novel cell adhesion. J Cell Sci 1996; 109: 2727-35.
- 15 Utani A, Ohta M, Shinya A, Ohno S, Takakuwa H, Yamamoto T, Suzaki T, Danno K. Successful treatment of adult Henoch-Schoenlein purpura with factor XIII concentrate. J Am Acad Dermatol 1991; 24: 438-42.
- 16 Wozniak G, Dapper F, Alemany J. Factor XIII in ulcerative leg disease: Background and preliminary clinical results. Semin Thromb Hemost 1996; 22: 445-50.
- 17 Wozniak G, Noll T, Dapper F, Piper HM, Hehrlein FW. Experimental approach to improve endothelial barrier function in myocardium. Int J Angiol 1999; 8: 119-23.