Isolation of a human endothelial cell C1q receptor (C1qR)

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Abstract
Clq 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 Clq receptor (ClqR) were used to isolate Clq 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 NHHerminal sequence as lymphocyte ClqR. This protein was expressed on the surface, as judged by surface radioiodination, bound to Clq-coated surfaces, and was recognized by polyclonal antilymphocyte ClqR antibodies. Thus, endothelial cells express a Clq receptor that appears identical to lymphocyte ClqR. The data further support the hypothesis that cell surface ClqRs identified on a variety of somatic and cultured cells are either identical or constitute a family of closely related molecules. J. Leukoc. Biol. 53: 179–184; 1993.

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