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C1qR_P Is a Heavily O-Glycosylated Cell Surface Protein Involved in the Regulation of Phagocytic Activity¹

Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697

C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) interact with human monocytes and macrophages, resulting in the enhancement of phagocytosis of suboptimally opsonized targets. mAbs that recognize a cell surface molecule of 126,000 M_r, designated C1qR_P, have been shown to inhibit C1q- and MBL-mediated enhancement of phagocytosis. Similar inhibition of the SPA-mediated enhancement of phagocytosis by these mAbs now suggests that C1qR_P is a common component of a receptor for these macromolecules. Ligation of human monocytes with immobilized R3, a IgM mAb recognizing C1qR_P, also triggers enhanced phagocytic capacity of these cells in the absence of ligand, verifying the direct involvement of this polypeptide in the regulation of phagocytosis. While the cDNA for C1qR_P encodes a 631 amino acid membrane protein, Chinese hamster ovary cells transfected with the cDNA of the C1qR_P coding region express a surface glycoprotein with the identical 126,000 M_r in SDS-PAGE as the native C1qR_P. Use of glycosylation inhibitors, cleavage of the mature C1qR_P with specific glycosidases, and in vitro translation of C1qR_P cDNA demonstrated that both posttranslational glycosylation and the nature of the amino acid sequence of the protein contribute to the difference between its predicted m.w. and its migration on SDS-PAGE. These results verify that the cDNA cloned codes for the mature C1qR_P, that C1qR_P contains a relatively high degree of O-linked glycoslyation, and that C1qR_P cross-linked directly by monoclonal anti-C1qR_P or engaged as a result of cell surface ligation of SPA, as well as C1q and MBL, enhances phagocytosis.

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