Zusammenfassung
Fibrin bildet die Proteinmatrix des Gerinnsels. Es wird durch Thrombin aus dem Plasmaprotein Fibrinogen gebildet. Grundbausteine des Fibrinogenmoleküls sind 3 Polypeptidketten: α-, β- und γ-Kette. Diese Fibrinogenketten werden durch 3 unterschiedliche Gene auf Chromosom 4 kodiert. Während der Fibrinogensynthese im Hepatozyten werden über N-terminale Disulfidbrücken Homodimere jeder Kette gebildet. Im Fibrinogenmolekül ist je 1 Homodimer jeder Kette so angeordnet, dass die N-terminalen Enden eine gemeinsame Molekülregion — die E-Domäne — bilden, während die beiden C-terminalen Enden die peripheren D-Domänen bilden. Thrombin spaltet die Fibrinopeptide A und B aus dem N-terminalen Bereich der α-und der β-Kette ab. Daraus resultiert eine Konformationsänderung, die ei Polymerisation der Fibrinogenmoleküle ermöglicht. Das entstehende Fibringerinnsel wird anschließnd durch aktivierten Faktor XIII kovalent vernetzt. Fibrin ist ein multivalenter Ligand für eine Reihe von zellulären Rezeptoren, zu denen auch die Integrine zählen. Ein Mangel an Fibrinogen tritt seltener angeboren und häufiger erworben im Zusammenhang mit verschiedenen Grunderkrankungen auf.
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Pötzsch, B., Madlener, K. (2010). Fibrinogen und Fibrin. In: Pötzsch, B., Madlener, K. (eds) Hämostaseologie. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-01544-1_22
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