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.
(Less)
- author
- Okrój, Marcin
LU
and Blom, Anna M.
LU
- organization
- publishing date
- 2017-10-19
- 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
- 2022-05-03 01:21:36
@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}},
keywords = {{CCP domain; Complement convertase autoimmunity; Complement inhibitor; Complement system}},
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}},
}