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DC Field | Value | Language |
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dc.contributor.author | Blackmore, T. | - |
dc.contributor.author | Hellwage, J. | - |
dc.contributor.author | Sadlon, T. | - |
dc.contributor.author | Higgs, N. | - |
dc.contributor.author | Zipfel, P. | - |
dc.contributor.author | Ward, H. | - |
dc.contributor.author | Gordon, D. | - |
dc.date.issued | 1998 | - |
dc.identifier.citation | Journal of Immunology, 1998; 160(7):3342-3348 | - |
dc.identifier.issn | 0022-1767 | - |
dc.identifier.issn | 1550-6606 | - |
dc.identifier.uri | http://hdl.handle.net/2440/81790 | - |
dc.description.abstract | Complement factor H (fH) regulates activation of the alternative pathway of C, reducing the amount of C3b deposited on sialic acid-rich surfaces. Heparin binding has been used as a model for examining the sialic acid- binding characteristics of fH. We have previously shown thai of the 20 short consensus repeat (SCR) modules of fH, SCR 7 contains an important heparin binding site, but other SCRs also play a role in heparin binding. To localize the other sites, we prepared recombinant truncated and SCR deletion mutants of fH and tested them by heparin-agarose affinity chromatography. The 5 C- terminal SCRs were found to contain a heparin binding site as an SCR 7 deletion mutant of the N terminal 15 SCRs did not bind heparin, but a construct consisting of SCRs 16-20 was shown to bind heparin. Double deletion of SCRs 7 and 20 fH abrogated binding to heparin, indicating that SCR 20 contains a heparin binding site. This finding was confirmed with the observation that attachment of SCR 20 to a group of nonbinding SCRs produced a heparin-binding protein. A protein consisting of SCRs 19 and 20 did not bind heparin, whereas SCRs 18-20 did, indicating that, although SCR 20 contains a heparin binding site, at least two nonspecific adjacent SCRs are required. fH-related protein-3 (FHR-3) possesses an SCR homologous to SCR 7 of fH and bound heparin, whereas FHR-4, which lacks such an SCR, did not. Thus, fH contains two separate heparin binding sites which are located in SCRs 7 and 20. | - |
dc.description.statementofresponsibility | Timothy K. Blackmore, Jens Hellwage, Tania A. Sadlon, Naomi Higgs, Peter F. Zipfel, Helena M. Ward, and David L. Gordon | - |
dc.language.iso | en | - |
dc.publisher | AMER ASSOC IMMUNOLOGISTS | - |
dc.rights | Copyright © 1998 by The American Association of Immunologists | - |
dc.source.uri | http://www.jimmunol.org/content/160/7/3342.abstract | - |
dc.subject | Humans | - |
dc.subject | Heparin | - |
dc.subject | Apolipoproteins | - |
dc.subject | Blood Proteins | - |
dc.subject | Complement Factor H | - |
dc.subject | Recombinant Proteins | - |
dc.subject | Sequence Deletion | - |
dc.subject | Binding Sites | - |
dc.subject | Repetitive Sequences, Nucleic Acid | - |
dc.subject | Consensus Sequence | - |
dc.subject | Protein Structure, Tertiary | - |
dc.title | Identification of a second heparin binding domain in human complement factor H | - |
dc.type | Journal article | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Ward, H. [0000-0002-3831-1205] | - |
Appears in Collections: | Aurora harvest 4 Medical Education Unit publications |
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