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Volume 271, Number 22, Issue of May 31, 1996 pp. 13040-13047
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Isolation and Characterization of the Kininogen-binding Protein p33 from Endothelial Cells
IDENTITY WITH THE gC1q RECEPTOR

(Received for publication, February 26, 1996, and in revised form, March 14, 1996)

Heiko Herwald ^§ , Jürgen Dedio ^§ , Roland Kellner ^§ , Michael Loos and Werner Müller-Esterl ^§

From the ^§ Institute for Physiological Chemistry and Pathobiochemistry and the  Institute of Medical Microbiology and Hygiene, Johannes Gutenberg University at Mainz, D-55099 Mainz, Federal Republic of Germany

Kininogens, the precursor proteins of the vasoactive kinins, bind specifically, reversibly, and saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5_H that is exclusively present in H-kininogen. Previously we have mapped the kininogen cell binding sites to 27 residues of D3 (``LDC27'') and 20 residues of D5<sub>H</sub> (``HKH20''), respectively (Herwald, H., Hasan, A. A. K., Godovac-Zimmermann, J., Schmaier, A. H., and Müller-Esterl, W. (1995) J. Biol. Chem. 270, 14634-14642; Hasan, A. A. K., Cines, D. B., Herwald, H., Schmaier, A. H., and Müller-Esterl, W. (1995) J. Biol. Chem. 270, 19256-19261). The corresponding kininogen acceptor site(s) exposed by the cell surfaces are still poorly defined. Using a non-ionic detergent, Nonidet P-40, we have been able to solubilize kininogen binding sites from an endothelial cell line, EA.hy926, in their functionally active form. Affinity chromatography of the solubilized kininogen binding sites on HKH20, a synthetic peptide representing the D5_H cell binding site, allowed us to isolate a 33-kDa protein (``p33'') that binds specifically and reversibly to H-kininogen with a K<sub>D</sub> (apparent dissociation constant) of 9 ± 2 nM. Preparative SDS electrophoresis followed by NH<sub>2</sub>-terminal amino acid sequence analysis identified the kininogen-binding protein p33 as the gC1q receptor (``gC1qR''), an extrinsic membrane protein that interacts with the globular domains of the complement component C1q. The purified p33 binds C1q with moderate affinity, K_D = 240 ± 10 nM. Recombinant expression of the corresponding cDNA in Escherichia coli demonstrated that p33 binds H-kininogen, but not L-kininogen. Peptide HKH20 but not peptide LDC27 inhibited binding of H-kininogen to the recombinant p33 in a concentration-dependent manner, indicating that H-kininogen binds to p33 via domain D5_H. Recombinant p33 efficiently inhibited the binding of H-kininogen to EA.hy926 cells. Factor XII, but not prekallikrein, competed with H-kininogen binding to p33. These findings suggest that an endothelial binding protein mediates the assembly of critical components of the kinin-generating pathway on the surface of endothelial cells, thereby linking the early events of kinin formation and complement activation.

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