Glycosylation is critical for natriuretic peptide receptor-B function

✍ Scribed by Randy Fenrick; Normand McNicoll; André Léan

• Book ID: 104673564
• Publisher: Springer
• Year: 1996
• Tongue: English
• Weight: 621 KB
• Volume: 165
• Category: Article
• ISSN: 0300-8177
• DOI: 10.1007/bf00229471

✦ Synopsis

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.