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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)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Molecular Immunology
volume
48
pages
1611 - 1620
publisher
Pergamon
external identifiers
  • wos:000294096100004
  • pmid:21529951
  • scopus:79960446438
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
2011-06-07 09:08:44
date last changed
2017-11-19 03:54:20
@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},
  series       = {Molecular Immunology},
  title        = {Complement factor I in health and disease.},
  url          = {http://dx.doi.org/10.1016/j.molimm.2011.04.004},
  volume       = {48},
  year         = {2011},
}