Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/14931
Title: C1 Complex: Structural Modularity and Functional Diversity
Authors: Lu, J
Kishore, U
Keywords: Complement;C1;autoimmunity;aging;infection;inflammation;C1q;macrophage;dendritic cell
Issue Date: 2017
Citation: Frontiers in Immunology
Abstract: Complement C1 is the defining component of the classical pathway. Within the C1qC1r2C1s2 complex, C1q functions as a molecular scaffold for C1r2C1s2 and C1q binding to its ligands activates these serine proteases. The classic C1q ligands are antibodies and activated C1s cleaves C4 and C2 to initiate the complement cascade. Recent studies suggest broad C1 functions beyond the complement system. C1q binds to Frizzled to activate C1s which cleaves LRP6 to trigger aging-associated Wnt receptor signalling. C1q binds to apoptotic cells and the activated C1 proteases cleave nuclear antigens. C1s also cleaves MHC class I molecule and potentially numerous other proteins. The diversity of C1q ligands and C1 protease substrates endorses C1 complex versatile and modular that can adapt to multiple molecular and cellular processes besides the complement system.
URI: http://bura.brunel.ac.uk/handle/2438/14931
ISSN: 1664-3224
Appears in Collections:Dept of Mechanical Aerospace and Civil Engineering Research Papers

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