Human complement C3 is a Substrate for Transglutaminases. A Functional Link between Non-Protease-Based Members of the Coagulation and Complement Cascades
| Autor: | Jan J. Enghild, Camilla Lund Nikolajsen, Carsten Scavenius |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Tissue transglutaminase
medicine.medical_treatment Biochemistry Fibrin Catalysis Substrate Specificity Plasma medicine Humans Amino Acid Sequence Binding site Blood Coagulation Complement Activation Protease Binding Sites Transglutaminases biology Chemistry Substrate (chemistry) Thrombosis Complement C3 Complement system Complement (complexity) Coagulation biology.protein Factor XIIIa |
| Zdroj: | Nikolajsen, C L, Scavenius, C & Enghild, J J 2012, ' Human complement C3 is a Substrate for Transglutaminases. A Functional Link between Non-Protease-Based Members of the Coagulation and Complement Cascades ', Biochemistry, vol. 51, no. 23, pp. 4735-4742 . https://doi.org/10.1021/bi3004022 |
| DOI: | 10.1021/bi3004022 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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