Isolation of a human endothelial cell C1q receptor (C1qR).

C1q binding to endothelial cells has been described previously, but the putative cell surface receptor(s) has not been identified. In the present study, modifications of a reported purification of lymphocyte C1q receptor (C1qR) were used to isolate C1q binding sites from human umbilical vein endothelial cells. Cells were harvested, without protease treatment, at passage 10-17 and lysed with 1% Triton X-100. The lysate was fractionated on Fast-performance liquid chromatography (FPLC) Mono-Q using a linear NaCl gradient, followed by high-performance liquid chromatography (HPLC) ion exchange (TSKgel DEAE-NPR). A major protein was eluted that had the same mobility on sodium dodecyl sulfate-polyacrylamide gels and the same NH2-terminal sequence as lymphocyte C1qR. This protein was expressed on the surface, as judged by surface radioiodination, bound to C1q-coated surfaces, and was recognized by polyclonal antilymphocyte C1qR antibodies. Thus, endothelial cells express a C1q receptor that appears identical to lymphocyte C1qR. The data further support the hypothesis that cell surface C1qRs identified on a variety of somatic and cultured cells are either identical or constitute a family of closely related molecules.