C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions

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 two serine proteases. The classic C1q ligands are antigen-bound antibodies and activated C1s cleaves C4...

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Main Authors: Jinhua Lu, Uday Kishore
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-05-01
Series:Frontiers in Immunology
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fimmu.2017.00592/full
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author Jinhua Lu
Uday Kishore
author_facet Jinhua Lu
Uday Kishore
author_sort Jinhua Lu
collection DOAJ
description 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 two serine proteases. The classic C1q ligands are antigen-bound 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 the Frizzled receptors to activate C1s, which cleaves lipoprotein receptor-related protein 6 to trigger aging-associated Wnt receptor signaling. 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 renders C1 complex versatile and modular so that it can adapt to multiple molecular and cellular processes besides the complement system.
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spelling doaj.art-fa9cadb503d34744b87fd5daef32686a2022-12-21T17:15:15ZengFrontiers Media S.A.Frontiers in Immunology1664-32242017-05-01810.3389/fimmu.2017.00592259880C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement FunctionsJinhua Lu0Uday Kishore1Department of Microbiology and Immunology, Yong Loo Lin School of Medicine and Immunology Programme, National University of Singapore, SingaporeDepartment of Life Sciences, College of Health and Life Sciences, Brunel University London, Uxbridge, UKComplement 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 two serine proteases. The classic C1q ligands are antigen-bound 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 the Frizzled receptors to activate C1s, which cleaves lipoprotein receptor-related protein 6 to trigger aging-associated Wnt receptor signaling. 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 renders C1 complex versatile and modular so that it can adapt to multiple molecular and cellular processes besides the complement system.http://journal.frontiersin.org/article/10.3389/fimmu.2017.00592/fullcomplement C1autoimmunityaginginfectioninflammationC1q
spellingShingle Jinhua Lu
Uday Kishore
C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
Frontiers in Immunology
complement C1
autoimmunity
aging
infection
inflammation
C1q
title C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
title_full C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
title_fullStr C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
title_full_unstemmed C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
title_short C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions
title_sort c1 complex an adaptable proteolytic module for complement and non complement functions
topic complement C1
autoimmunity
aging
infection
inflammation
C1q
url http://journal.frontiersin.org/article/10.3389/fimmu.2017.00592/full
work_keys_str_mv AT jinhualu c1complexanadaptableproteolyticmoduleforcomplementandnoncomplementfunctions
AT udaykishore c1complexanadaptableproteolyticmoduleforcomplementandnoncomplementfunctions