Complement factor I in health and disease.
Nilsson, Sara LU ; Sim, Robert B ; Lea, Susan M ; Fremeaux-Bacchi, Veronique and Blom, Anna LU
(2011)
In Molecular Immunology
48.
p.1611-1620
- Abstract
- Factor I (FI) is a crucial inhibitor controlling all complement pathways due to its ability to degrade activated complement proteins C3b and C4b in the presence of cofactors such as factor H, C4b-binding protein, complement receptor 1 or CD46. Complete deficiency of FI, which is synthesized mainly in the liver is rare and leads to complement consumption resulting in recurrent severe infections, glomerulonephritis or autoimmune diseases. Incomplete FI deficiency is in turn associated with atypical haemolytic uremic syndrome, a severe disease characterized by thrombocytopenia, microangiopathic haemolytic anaemia and acute renal failure. Structurally, FI is a 88kDa heterodimer of a heavy chain consisting of one FI-membrane attack complex... (More)
- Factor I (FI) is a crucial inhibitor controlling all complement pathways due to its ability to degrade activated complement proteins C3b and C4b in the presence of cofactors such as factor H, C4b-binding protein, complement receptor 1 or CD46. Complete deficiency of FI, which is synthesized mainly in the liver is rare and leads to complement consumption resulting in recurrent severe infections, glomerulonephritis or autoimmune diseases. Incomplete FI deficiency is in turn associated with atypical haemolytic uremic syndrome, a severe disease characterized by thrombocytopenia, microangiopathic haemolytic anaemia and acute renal failure. Structurally, FI is a 88kDa heterodimer of a heavy chain consisting of one FI-membrane attack complex (FIMAC) domain, one CD5 domain and two low-density lipoprotein receptor domains (LDLr), and a light chain which is a serine protease domain (SP), linked to the heavy chain by a disulfide bond. FI cleaves its in vivo substrates C3b and C4b only in the presence of cofactors, it shows poor enzymatic activity towards synthetic substrates tested so far and it has no natural inhibitor. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1973336
- author
- Nilsson, Sara
LU
; Sim, Robert B
; Lea, Susan M
; Fremeaux-Bacchi, Veronique
and Blom, Anna
LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Immunology
- volume
- 48
- pages
- 1611 - 1620
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- wos:000294096100004
- pmid:21529951
- scopus:79960446438
- pmid:21529951
- ISSN
- 1872-9142
- DOI
- 10.1016/j.molimm.2011.04.004
- language
- English
- LU publication?
- yes
- id
- f6d06d32-8000-4b31-9bb5-b6dcd4fe2277 (old id 1973336)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21529951?dopt=Abstract
- date added to LUP
- 2016-04-01 14:14:09
- date last changed
- 2022-05-19 23:31:07
@article{f6d06d32-8000-4b31-9bb5-b6dcd4fe2277,
abstract = {{Factor I (FI) is a crucial inhibitor controlling all complement pathways due to its ability to degrade activated complement proteins C3b and C4b in the presence of cofactors such as factor H, C4b-binding protein, complement receptor 1 or CD46. Complete deficiency of FI, which is synthesized mainly in the liver is rare and leads to complement consumption resulting in recurrent severe infections, glomerulonephritis or autoimmune diseases. Incomplete FI deficiency is in turn associated with atypical haemolytic uremic syndrome, a severe disease characterized by thrombocytopenia, microangiopathic haemolytic anaemia and acute renal failure. Structurally, FI is a 88kDa heterodimer of a heavy chain consisting of one FI-membrane attack complex (FIMAC) domain, one CD5 domain and two low-density lipoprotein receptor domains (LDLr), and a light chain which is a serine protease domain (SP), linked to the heavy chain by a disulfide bond. FI cleaves its in vivo substrates C3b and C4b only in the presence of cofactors, it shows poor enzymatic activity towards synthetic substrates tested so far and it has no natural inhibitor.}},
author = {{Nilsson, Sara and Sim, Robert B and Lea, Susan M and Fremeaux-Bacchi, Veronique and Blom, Anna}},
issn = {{1872-9142}},
language = {{eng}},
pages = {{1611--1620}},
publisher = {{Pergamon Press Ltd.}},
series = {{Molecular Immunology}},
title = {{Complement factor I in health and disease.}},
url = {{https://lup.lub.lu.se/search/files/3858116/2018925.pdf}},
doi = {{10.1016/j.molimm.2011.04.004}},
volume = {{48}},
year = {{2011}},
}