Glycosylation is critical for natriuretic peptide receptor-B function.
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.
Fenrick
R
R
Department of Pharmacology, University of Montreal, Quebec, Canada.
McNicoll
N
N
De Léan
A
A
D000818:Animals; D015153:Blotting, Western; D019556:COS Cells; D002417:Cattle; D003432:Cross-Linking Reagents; D006152:Cyclic GMP / Q000378:metabolism; D006031:Glycosylation; D006162:Guanylate Cyclase / Q000235:genetics / Q000378:metabolism*; D018343:Receptors, Adrenergic, beta-2 / Q000235:genetics / Q000378:metabolism; D017461:Receptors, Atrial Natriuretic Factor / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D014162:Transfection; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D018343:Receptors, Adrenergic, beta-2; D006162:Guanylate Cyclase; D017461:Receptors, Atrial Natriuretic Factor; C073616:atrial natriuretic factor receptor C; D006152:Cyclic GMP