Aarhus University Seal / Aarhus Universitets segl

Carsten Scavenius

Human complement C3 is a Substrate for Transglutaminases. A Functional Link between Non-Protease-Based Members of the Coagulation and Complement Cascades

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

In this study, we report the finding of functional cross-talk between two non-protease components of the complement and coagulation cascades. We show that complement C3, a central component of the complement system, is associated with the fibrin clot and that C3 becomes covalently cross-linked to other proteins during coagulation. Enzymatic incorporation of dansylcadaverine and dansyl-PGGQQIV into C3 by coagulation factor XIIIa and tissue transglutaminase demonstrated that C3 is a transglutaminase substrate. This suggested that coagulation factor XIIIa covalently cross-links C3 to clot components during coagulation. Using mass spectrometry, we verified that C3 indeed is covalently associated with the fibrin clot in a ratio of 0.05:1 relative to the known coagulation factor XIIIa substrate α2-antiplasmin.
Original languageEnglish
JournalBiochemistry
Volume51
Issue23
Pages (from-to)4735-4742
Number of pages8
ISSN0006-2960
DOIs
Publication statusPublished - 25 May 2012

    Research areas

  • Amino Acid Sequence, Binding Sites, Blood Coagulation, Catalysis, Complement Activation, Complement C3, Factor XIIIa, Humans, Plasma, Substrate Specificity, Thrombosis, Transglutaminases

See relations at Aarhus University Citationformats

ID: 48769123