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Article: The binding protein for globular heads of complement C1q, gC1qR: Functional expression and characterization as a novel vitronectin binding factor

TitleThe binding protein for globular heads of complement C1q, gC1qR: Functional expression and characterization as a novel vitronectin binding factor
Authors
Issue Date1996
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1996, v. 271 n. 43, p. 26739-26744 How to Cite?
AbstractA binding protein for the globular head domains of complement component C1q, designated gC1qR, recently described to be present on vascular and blood cells (Ghebrehiwet, B., Lim, B.-L., Peerschke, E. I. B., Willis, A. C., and Reid, K. B. M. (1994) J. Exp. Med. 179, 1809-1821 was expressed in recombinant form in bacteria to investigate its functional and structural properties. The recombinant gC1qR was found to be functional because tetramerization of the 24.3-kDa polypeptide occurred as described for the native protein, and the binding of the ligand C1q by recombinant gC1qR was indistinguishable from binding shown by gC1qR isolated from Raji cells. Recombinant gC1qR immobilized to microspheres was used to search for additional binding proteins unrelated to C1q. Surprisingly, it was found that vitronectin or complexes containing vitronectin were retained from plasma or serum, and subsequent analysis revealed the specific binding of the ternary vitronectin-thrombin-antithrombin complex to gC1qR. Because the thrombin- antithrombin complex was unable to interact with gC1qR, direct binding with vitronectin was investigated in a purified system. The heparin binding multimeric form of vitronectin but not the plasma form of vitronectin was found to bind specifically to gC1qR isolated from Raji cell membrane as well as to recombinant gC1qR. This interaction was saturable (K(D) -20 nM) and inhibitable by glycosaminoglycans such as heparin but not by chondroitin sulfate. C1q and vitronectin did not compete with each other for binding to gC1qR, and both ligands seem to interact with different parts of the gC1qR because a truncated version of recombinant gC1qR lacking the N-terminal 22- amino acid portion hardly interacted with vitronectin but bound C1q as well as the intact gC1qR. These findings establish gC1qR as a novel vitronectin- binding protein that may participate in the clearance of vitronectin- containing complexes or opsonized particles or cooperate with vitronectin in the inhibition of complement-mediated cytolysis.
Persistent Identifierhttp://hdl.handle.net/10722/49430
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLim, BLen_HK
dc.contributor.authorReid, KBMen_HK
dc.contributor.authorGhebrehiwet, Ben_HK
dc.contributor.authorPeerschke, EIBen_HK
dc.contributor.authorLeigh, LAEen_HK
dc.contributor.authorPreissner, KTen_HK
dc.date.accessioned2008-06-12T06:42:28Z-
dc.date.available2008-06-12T06:42:28Z-
dc.date.issued1996en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1996, v. 271 n. 43, p. 26739-26744en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49430-
dc.description.abstractA binding protein for the globular head domains of complement component C1q, designated gC1qR, recently described to be present on vascular and blood cells (Ghebrehiwet, B., Lim, B.-L., Peerschke, E. I. B., Willis, A. C., and Reid, K. B. M. (1994) J. Exp. Med. 179, 1809-1821 was expressed in recombinant form in bacteria to investigate its functional and structural properties. The recombinant gC1qR was found to be functional because tetramerization of the 24.3-kDa polypeptide occurred as described for the native protein, and the binding of the ligand C1q by recombinant gC1qR was indistinguishable from binding shown by gC1qR isolated from Raji cells. Recombinant gC1qR immobilized to microspheres was used to search for additional binding proteins unrelated to C1q. Surprisingly, it was found that vitronectin or complexes containing vitronectin were retained from plasma or serum, and subsequent analysis revealed the specific binding of the ternary vitronectin-thrombin-antithrombin complex to gC1qR. Because the thrombin- antithrombin complex was unable to interact with gC1qR, direct binding with vitronectin was investigated in a purified system. The heparin binding multimeric form of vitronectin but not the plasma form of vitronectin was found to bind specifically to gC1qR isolated from Raji cell membrane as well as to recombinant gC1qR. This interaction was saturable (K(D) -20 nM) and inhibitable by glycosaminoglycans such as heparin but not by chondroitin sulfate. C1q and vitronectin did not compete with each other for binding to gC1qR, and both ligands seem to interact with different parts of the gC1qR because a truncated version of recombinant gC1qR lacking the N-terminal 22- amino acid portion hardly interacted with vitronectin but bound C1q as well as the intact gC1qR. These findings establish gC1qR as a novel vitronectin- binding protein that may participate in the clearance of vitronectin- containing complexes or opsonized particles or cooperate with vitronectin in the inhibition of complement-mediated cytolysis.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshAntigens, CD44en_HK
dc.subject.meshComplement C1q - metabolismen_HK
dc.subject.meshMembrane Glycoproteinsen_HK
dc.subject.meshReceptors, Complement - genetics - isolation & purification - metabolismen_HK
dc.subject.meshReceptors, Vitronectin - genetics - metabolismen_HK
dc.titleThe binding protein for globular heads of complement C1q, gC1qR: Functional expression and characterization as a novel vitronectin binding factoren_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=271&issue=43&spage=26739&epage=26744&date=1996&atitle=The+binding+protein+for+globular+heads+of+complement+C1q,+gC1qR:+functional+expression+and+characterization+as+a+novel+vitronectin+binding+factoren_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1074/jbc.271.43.26739en_HK
dc.identifier.pmid8900153-
dc.identifier.scopuseid_2-s2.0-0029910212en_HK
dc.identifier.hkuros21990-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029910212&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume271en_HK
dc.identifier.issue43en_HK
dc.identifier.spage26739en_HK
dc.identifier.epage26744en_HK
dc.identifier.isiWOS:A1996VP23300047-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK
dc.identifier.scopusauthoridReid, KBM=7202780648en_HK
dc.identifier.scopusauthoridGhebrehiwet, B=7005039582en_HK
dc.identifier.scopusauthoridPeerschke, EIB=7005991940en_HK
dc.identifier.scopusauthoridLeigh, LAE=55409362100en_HK
dc.identifier.scopusauthoridPreissner, KT=7007034391en_HK

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