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Hamostaseologie 1994; 14(04): 184-189
DOI: 10.1055/s-0038-1660362
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Fibrinogen-Varianten: Biochemie, Molekularbiologie und Diagnostik

Agnes H. Henschen
1   Department of Molecular Biology and Biochemistry, University of California, Irvine, USA
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Publication Date:
26 June 2018 (online)

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Zusammenfassung

Das humane Fibrinogen hat ein Molekulargewicht von 340 kD und eine Struktur, die mit (Aα, Bβ, γ)2 beschrieben werden kann. Es ist ein außerordentlich heterogenes Protein, da zahlreiche Bereiche des Moleküls während oder nach der Biosynthese modifiziert werden, die Modifikationen gewöhnlich unvollständig sind und in einzelnen Molekülen unterschiedlich kombiniert sein können. Die bis jetzt bekannten Modifikationen sind: alternative Prozessierung bei der Synthese, Phosphorylierung, Sulfatierung, Hydroxylierung, Oxidierung, Amid-AmmoniakVerlust, Glykosylierung, proteolytischer Abbau und genetischer Polymorphismus. Hieraus kann berechnet werden, daß das Fibrinogen in mehr als einer Million nichtidentischer Formen im Blut jedes Menschen vorhanden ist. Bei einigen Modifikationen ist eine Beziehung zu Erkrankungen bekannt. Zusätzliche Modifikationen entstehen durch Mutationen und führen zu Dysfibrinogenämien, die schon bei mehr als 80 Familien in ihrer Struktur aufgeklärt wurden.

Schlüsselwörter

Fibrinogen - Variante - Polymorphismus - genetische Variante - Heterogenität - Risikofaktor - Herz-Kreislauf-Krankheit - Phosphorylierung - Sulfatierung - Glykosylierung
 

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