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C4b-Binding Protein

Okrój, Marcin LU and Blom, Anna M. LU (2017) p.251-259
Abstract

C4b-binding protein (C4BP) is the main fluid-phase inhibitor of the classical complement pathway. It serves as cofactor in factor I-mediated cleavage of C4b and C3b and it accelerates the decay of complement convertases. The main role of C4BP is to prevent overt complement-mediated inflammation both in solution and on self-molecules recognised by C1q, such as amyloid. Furthermore, C4BP is frequently recruited onto the surface of various pathogens, which allows these to evade immune response. The main isoform of C4BP has a oligomeric structure and consists of seven chains, which confer complement inhibitory activity, and a single chain, which binds anticoagulant protein S and docks the molecule to negatively charged phospholipids... (More)

C4b-binding protein (C4BP) is the main fluid-phase inhibitor of the classical complement pathway. It serves as cofactor in factor I-mediated cleavage of C4b and C3b and it accelerates the decay of complement convertases. The main role of C4BP is to prevent overt complement-mediated inflammation both in solution and on self-molecules recognised by C1q, such as amyloid. Furthermore, C4BP is frequently recruited onto the surface of various pathogens, which allows these to evade immune response. The main isoform of C4BP has a oligomeric structure and consists of seven chains, which confer complement inhibitory activity, and a single chain, which binds anticoagulant protein S and docks the molecule to negatively charged phospholipids exposed, e.g., on the surface of dying cells. Both α- and β- chains are built from complement control protein (CCP) domains typical of complement inhibitors. C4BP is one of the acute-phase proteins and its expression is upregulated by proinflammatory cytokines.

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Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
keywords
CCP domain, Complement convertase autoimmunity, Complement inhibitor, Complement system
host publication
The Complement FactsBook : Second Edition - Second Edition
pages
9 pages
publisher
Elsevier
external identifiers
  • scopus:85041254052
ISBN
9780128104200
DOI
10.1016/B978-0-12-810420-0.00024-9
language
English
LU publication?
yes
id
ca6bd17d-7fd7-4857-990e-68ccaf99f92d
date added to LUP
2018-02-12 14:27:47
date last changed
2020-09-16 03:40:01
@inbook{ca6bd17d-7fd7-4857-990e-68ccaf99f92d,
  abstract     = {<p>C4b-binding protein (C4BP) is the main fluid-phase inhibitor of the classical complement pathway. It serves as cofactor in factor I-mediated cleavage of C4b and C3b and it accelerates the decay of complement convertases. The main role of C4BP is to prevent overt complement-mediated inflammation both in solution and on self-molecules recognised by C1q, such as amyloid. Furthermore, C4BP is frequently recruited onto the surface of various pathogens, which allows these to evade immune response. The main isoform of C4BP has a oligomeric structure and consists of seven chains, which confer complement inhibitory activity, and a single chain, which binds anticoagulant protein S and docks the molecule to negatively charged phospholipids exposed, e.g., on the surface of dying cells. Both α- and β- chains are built from complement control protein (CCP) domains typical of complement inhibitors. C4BP is one of the acute-phase proteins and its expression is upregulated by proinflammatory cytokines.</p>},
  author       = {Okrój, Marcin and Blom, Anna M.},
  booktitle    = {The Complement FactsBook : Second Edition},
  isbn         = {9780128104200},
  language     = {eng},
  month        = {10},
  pages        = {251--259},
  publisher    = {Elsevier},
  title        = {C4b-Binding Protein},
  url          = {http://dx.doi.org/10.1016/B978-0-12-810420-0.00024-9},
  doi          = {10.1016/B978-0-12-810420-0.00024-9},
  year         = {2017},
}