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Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

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Cell surface expression of C1qRP/CD93 is stabilized by O-glycosylation

Minha Park1, Andrea J Tenner

  • 1Department of Molecular Biology & Biochemistry, University of California, Irvine, California 92697-3900, USA.

Journal of Cellular Physiology
|August 2, 2003
PubMed

C1qRP/CD93 is a cell surface receptor predominantly expressed on monocytes, neutrophils, endothelial cells, and early stem cell precursors. In phagocytic cells, it has been characterized as contributing to the enhancement of FcR- and CR1-induced phagocytosis triggered by innate immune system defense collagens such as C1q and mannose binding lectin (MBL). Previously, we demonstrated a high level of glycosylation on C1qRP/CD93 that was predominantly O-linked. In this study, we investigate the role of glycosylation in C1qRP/CD93 stability first by inhibiting O-glycosylation by addition of benzyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside (BAG) to the human histiocytic cell line U937, and secondly, by expression of C1qRP/CD93 in the CHO-derived cell line ldlD which has a reversible defect in protein glycosylation. In both U937 cells and in ldlD cells transfected to express C1qRP/CD93, glycosylation deficiency caused cell surface expression levels of C1qRP/CD93 to decrease, concomitant with the detection of C1qRP/CD93 reactivity in the culture media. Metabolic labeling studies show that when glycosylation is absent, C1qRP/CD93 is synthesized and rapidly released into the culture supernatant or degraded. These studies demonstrate that O-glycosylation is important in the stable cell surface expression of C1qRP/CD93 .

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