Human complement factor H: two factor H proteins are derived from alternatively spliced transcripts

Estaller, Cornelia; Schwaeble, Wilhelm; Dierich, Manfred P.; Weiß, Elisabeth H.

doi:10.1002/eji.1830210337

Cited by 85 publications

(54 citation statements)

References 22 publications

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“…For example, the two C-terminal SCRs in all FHR proteins show strong homology to the corresponding SCRs of Factor H. In contrast, the two N-terminal SCRs of FHR-1 and FHR-2 (Fig. 9, A and B) appear to be unrelated to the SCRs of Factor H (13,14,30). FHR-5 is most similar to FHR-2 but is unique among the FHR proteins in that it contains five additional SCRs, homologous to SCRs 10 -14 of Factor H, which are not present in the other FHR proteins.…”

Section: Table III Amino Acid Homology Of Hplc-purified Peptides To Tmentioning

confidence: 99%

Human Factor H-related Protein 5 (FHR-5)

McRae¹,

Cowan²,

Power³

et al. 2001

Journal of Biological Chemistry

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A novel human plasma protein has been identified as a universal component of complement deposits, when complement is detected immunohistochemically in vivo. The protein is homologous to complement factor H and related proteins and has been designated factor H-related protein 5 (FHR-5). FHR-5 was identified by a monoclonal antibody raised using pathologic human glomerular preparations as the immunogen. FHR-5 was purified by affinity chromatography from complementlysed erythrocytes, and the peptide sequence was obtained. The cDNA was cloned from a human liver library, and FHR-5 was deduced to be a protein containing 551 amino acids organized into nine short consensus repeat motifs. The short consensus repeats of FHR-5 show homology to Factor H and to other Factor H-related proteins, with some unique features demonstrated. Recombinant FHR-5, expressed in insect cells, was shown to bind C3b in vitro. The strong association of FHR-5 with tissue complement deposits in vivo suggests that this additional member of the Factor H family of proteins has a function in complement regulation.

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Section: Table III Amino Acid Homology Of Hplc-purified Peptides To Tmentioning

confidence: 99%

Human Factor H-related Protein 5 (FHR-5)

McRae¹,

Cowan²,

Power³

et al. 2001

Journal of Biological Chemistry

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“…A human liver cDNA library constructed in the eukaryotic expression vector CDM8 [9] was screened with an IL-lra probe derived from HepG2 mRNA by PCR. The length of the positive cDNA clones was estimz ..d by a Pstl.Hindlll restriction digest.…”

Section: Isolation Of Ll-lra Clones and Edna Sequencingmentioning

confidence: 99%

Human interleukin‐1 receptor antagonist is expressed in liver

Steinkasserer

Estaller²,

Weiß³

et al. 1992

FEBS Letters

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“…It is a glycoprotein in human plasma composed of 20 repetitive units of 60 aa, which is designated complement control protein domains or short consensus repeats (SCRs) (20). Another regulator of the alternative pathway is the FHL-1, which is a product of alternative splicing of the FH gene (21). FHL-1 is a 42-kDa protein composed of seven SCRs identical with the N-terminal SCRs of FH and includes an extension of 4 aa at its C-terminal end (16).…”

mentioning

confidence: 99%

Haemophilus influenzae Interacts with the Human Complement Inhibitor Factor H

Hallström

Zipfel

Blom

et al. 2008

The Journal of Immunology

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Pathogenic microbes acquire human complement inhibitors to circumvent the innate immune system. In this study, we identify two novel host-pathogen interactions, factor H (FH) and factor H-like protein 1 (FHL-1), the inhibitors of the alternative pathway that binds to Hib. A collection of clinical Haemophilus influenzae isolates was tested and the majority of encapsulated and unencapsulated bound FH. The isolate Hib 541 with a particularly high FH-binding was selected for detailed analysis. An increased survival in normal human serum was observed with Hib 541 as compared with the low FH-binding Hib 568. Interestingly, two binding domains were identified within FH; one binding site common to both FH and FHL-1 was located in the N-terminal short consensus repeat domains 6–7, whereas the other, specific for FH, was located in the C-terminal short consensus repeat domains 18–20. Importantly, both FH and FHL-1, when bound to the surface of Hib 541, retained cofactor activity as determined by analysis of C3b degradation. Two H. influenzae outer membrane proteins of ∼32 and 40 kDa were detected with radiolabeled FH in Far Western blot. Taken together, in addition to interactions with the classical, lectin, and terminal pathways, H. influenzae interferes with the alternative complement activation pathway by binding FH and FHL-1, and thereby reducing the complement-mediated bactericidal activity resulting in an increased survival. In contrast to incubation with active complement, H. influenzae had a reduced survival in FH-depleted human serum, thus demonstrating that FH mediates a protective role at the bacterial surface.

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Human complement factor H: two factor H proteins are derived from alternatively spliced transcripts

Cited by 85 publications

References 22 publications

Human Factor H-related Protein 5 (FHR-5)

Human Factor H-related Protein 5 (FHR-5)

Human interleukin‐1 receptor antagonist is expressed in liver

Haemophilus influenzae Interacts with the Human Complement Inhibitor Factor H

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