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Volume 271, Number 43, Issue of October 25, 1996 pp. 26739-26744
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Binding Protein for Globular Heads of Complement C1q, gC1qR
FUNCTIONAL EXPRESSION AND CHARACTERIZATION AS A NOVEL VITRONECTIN BINDING FACTOR

(Received for publication, January 22, 1996, and in revised form, July 17, 1996)

Boon-Leong Lim , Kenneth B. M. Reid ^§ , Berhane Ghebrehiwet ^¶ , Ellinor I. B. Peerschke ^¶ , Leonora A. E. Leigh ^§ and Klaus T. Preissner

From the  Department of Zoology, The University of Hong Kong, Pokfulam, Hong Kong, ^§ Medical Research Center Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom, ^¶ Departments of Medicine and Pathology, State University of New York, Stony Brook, New York 11794-8161, and  Haemostasis Research Unit, Kerckhoff-Klinik, Max-Planck-Institut, D-61231 Bad Nauheim, Germany

A 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.

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