Factor H

Vik, D P; Muñoz‐Cánoves, Pura; Chaplin, David; Tack, Brian F.

doi:10.1007/978-3-642-74977-3_8

Cited by 34 publications

(27 citation statements)

References 83 publications

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“…SCR elements represent a common structural motif of about 60 amino acids and are found in several complement regulatory proteins that interact with and regulate C3b and C4b [4]. Among the members of the H protein family, complement regulatory functions have been described for fH [5] and FHL-1 [6,7], but not for any of the FHR proteins. fH and FHL-1 act as cofactor for factor-I-mediated degradation of C3b, and both proteins have decay-accelerating activity [6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

Prodinger

Hellwage

Spruth

et al. 1998

Molecular Immunology

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Section: Introductionmentioning

confidence: 99%

The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

Prodinger

Hellwage

Spruth

et al. 1998

Molecular Immunology

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“…Factor H is a 150 kDa plasma protein that regulates the alternative pathway of complement activation [6]. It binds to C3b and accelerates the dissociation of Bb, thereby disrupting the C3 convertase activity.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Williams

Vik

1997

Scand J Immunol

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Williams SA, Vik DP. Characterization of the 5 0 Flanking Region of the Human Complement Factor H Gene. Scand J Immunol 1997;45:7-15 The promoter region of the human factor H gene was cloned and a 3 kb Eco RI fragment was sequenced. Primer extension and S1 nuclease analysis were used to determine the transcription start site, which was found to be 10-11 nucleotides upstream of the published cDNA sequence. No canonical TATA or CCAAT boxes were found in conjunction with this site. The sequence from the human H promoter region was compared to that from the mouse gene. There was a region of 800 bp that was 62.5% identical between the two sequences. The sequences of the two promoter regions were compared to a database of transcription factor binding sites. Five elements were identified that matched the consensus sequence 100% and were identical in the two promoter sequences. Promoter assays using the luciferase reporter gene demonstrated that this region contained a functional transcription start site and putative enhancer elements. U118-MG astroglioma cells and Hep3b hepatoma cells were incubated with various cytokines to measure effects on their factor H mRNA levels. Interferon-(IFN-), but not interleukin-1 (IL-1), tumour necrosis factor (TNF-) or IL-6, was able to increase the level of H mRNA in both cell lines.

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“…These structures have been recognized in 12 complement proteins and many noncomplement proteins including blood-clotting factor XIIIb, the ␣-chain of the interleukin-2 receptor, and cell adhesion molecules such as endothelial leukocyte adhesion molecule-1 and leukocyte adhesion molecule-1. The SCR motifs define a protein superfamily (10), characterized by conserved tyrosine, proline, and glycine residues and by the presence of four conserved cysteine residues, which form two disulfide bridges in a Cys 1 -Cys 3 and Cys 2 -Cys 4 fashion (11,12). The 20 SCR modules of factor H are joined by short (3-8-amino acid) linkers, resulting in a shape that resembles a string of beads (13).…”

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Disruption of Disulfide Bonds Is Responsible for Impaired Secretion in Human Complement Factor H Deficiency

Schmidt

Fowler

Hidvegi

et al. 1999

Journal of Biological Chemistry

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Factor H, a secretory glycoprotein composed of 20 short consensus repeat modules, is an inhibitor of the complement system. Previous studies of inherited factor H deficiency revealed single amino acid substitutions at conserved cysteine residues, on one allele arginine for cysteine 518 (C518R) and on the other tyrosine for cysteine 941 (C941Y) (Ault, B. H., Schmidt, B. Z., Fowler, N. L., Kashtan, C. E., Ahmed, A. E., Vogt, B. A., and Colten, H. R. (1997) J. Biol. Chem. 272, 25168 -25175). To ascertain if the phenotype, impaired secretion of factor H, is due to the C518R substitution or the C941Y substitution and to ascertain the mechanism by which secretion is impaired, we studied COS-1 and HepG2 cells transfected with wild type and several mutant factor H molecules. The results showed markedly impaired secretion of both C518R and C941Y factor H as well as that of factor H molecules bearing alanine or arginine substitutions at the Cys 518 -Cys 546 disulfide bond (C518A, C546A, C546R, C518A-C546A). In each case, mutant factor H was retained in the endoplasmic reticulum and degraded relatively slowly as compared with most other mutant secretory and membrane proteins that are retained in the endoplasmic reticulum. These data indicate that impaired secretion of the naturally occurring C518R and C941Y mutant factor H proteins is due to disruption of framework-specific disulfide bonds in factor H short consensus repeat modules.

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Factor H

Cited by 34 publications

References 83 publications

The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

Characterization of the 5′ Flanking Region of the Human Complement Factor H Gene

Disruption of Disulfide Bonds Is Responsible for Impaired Secretion in Human Complement Factor H Deficiency

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