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Mol Cell Biochem. 1996 Dec 20;165(2):103-9.

Glycosylation is critical for natriuretic peptide receptor-B function.

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Department of Pharmacology, University of Montreal, Quebec, Canada.


Co-transfection of a truncated natriuretic peptide receptor-B (NPR-B) with the full length receptor results in a decrease of 60-80% in wild-type receptor activity. This reduction correlates with a loss of glycosylation of the full length NPR-B. This effect is dose-dependent, and occurs with no change in the glycosylation of the truncated receptor. Co-transfection of the full length NPR-B with other receptors yields similar results. These data suggest that glycosylation may be crucial for NPR-B function. Cross-linking studies further demonstrate that only fully glycosylated NPR-B receptors are able to bind ligand. Our data therefore argue that carbohydrate modification may be critical for NPR-B receptor ligand binding.

[Indexed for MEDLINE]

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