Abstract
Here we summarize our biochemical and histochemical characterization of L-selectin ligands in the kidney. The staining pattern with anti-sialyl LeX antibodies (KM-93, FH-6 and CSLEX-1) was distinct from that with L-selectin-IgG chimera (LEC-IgG), suggesting that sialyl LeX antigen is not associated with ligands for L-selectin in the kidney, unlike other glycoprotein ligands for L-selectin. Immuno-precipitation analysis with LEC-IgG revealed that a proteoglycan-like molecule from a renal tubule-derived cell line specifically bound to L-selectin. Using sequential column chromatography, we isolated this proteoglycan-like molecule and identified it as versican, a large chondroitin sulfate proteoglycan. Histochemical examination confirmed that versican is localized in the distal straight tubules of the rat kidney where L-selectin ligands are detected. Interestingly, after ureteral obstruction in the rat, versican disappeared from the renal tubules and appeared in the vascular bundles. Concomitantly, a massive leukocyte infiltration was observed around the vascular bundles, which was significantly inhibited with administration of an anti -L-selectin monoclonal antibody. These results suggest that versican secluded in the renal tubules under physiological conditions may play a role in leukocyte infiltration as an L-selectin ligand by changing its localization under pathological conditions.
