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N-glycosylation plays a role in biosynthesis and internalization of the adenylate cyclase stimulating vasopressin V2-receptor of LLC-PK1 renal epithelial cells: an effect of concanavalin A on binding and expression

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Jans,  David A.
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Jans,  Patricia
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Luzius,  Heike
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fahrenholz,  Falk
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Jans, D. A., Jans, P., Luzius, H., & Fahrenholz, F. (1992). N-glycosylation plays a role in biosynthesis and internalization of the adenylate cyclase stimulating vasopressin V2-receptor of LLC-PK1 renal epithelial cells: an effect of concanavalin A on binding and expression. Archives of Biochemistry and Biophysics, 294(1), 64-69. doi:10.1016/0003-9861(92)90137-l.


Cite as: https://hdl.handle.net/21.11116/0000-0007-EB2A-2
Abstract
The role of N-glycosylation in the function and biosynthesis of the vasopressin V2-receptor in LLC-PK1 renal epithelial cells was examined using various lectins and inhibitors operating at different steps of the glycosidic pathway. Tunicamycin, which blocks all N-glycosylation, and castanospermine, which inhibits glycosidase I and hence blocks formation of high-mannose-type N-glycosylated intermediates, resembled one another in affecting V2-receptor biosynthesis and internalization in a concentration-dependent manner. In contrast, swainsonine, an inhibitor of mannosidase II and hence of complex-type oligosaccharide formation, had no effect. Interestingly, the alpha-D-mannose/alpha-D-glucose-specific lectin concanavalin A, (Con A), in contrast to the beta-D-galactose-specific lectin ricin, had a marked effect on the V2-receptor in LLC-PK1 cells, increasing both receptor numbers up to twofold in vivo and specific [3H]AVP binding up to 50% in vitro in a concentration-dependent manner. The concentrations inducing half-maximal response were about 0.2 and 20 micrograms/ml for the in vivo and in vitro responses, respectively, implying distinct effects on V2-expression and ligand binding. That the in vitro effect on binding was due to a direct effect on the V2-receptor could be shown by the lack of a Con A effect on [3H]AVP binding in membranes prepared from LLC-PK1 cells down-regulated for the V2-receptor or from cells of the LLC-PK1 V2-receptor deficient mutant M18. All results were consistent with a functional role for N-glycosylation of the V2-receptor in LLC-PK1 cells.