Characterization of the phosphorylation state of natriuretic peptide receptor-C |
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Authors: | Pedro Liliana Fenrick Randy Marquis Martin McNicoll Normand De Léan André |
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Institution: | (1) Département de Pharmacologie, Université de Montréal, Montréal, Québec, H3C 3J7, Canada;(2) Département de Biochimie, Université de Montréal, Montréal, Québec, H3C 3J7, Canada |
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Abstract: | Many internalized receptors are known to be phosphorylated within their cytoplasmic domain. Natriuretic peptide receptor-C (NPR-C) is a covalent homodimer primarily involved in the internalization of bound ligand resulting in tissue uptake and degradation of natriuretic peptides. In this report, we have investigated the phosphorylation state of NPR-C receptors present at high level in rat aortic smooth muscle cells (RASM).32 P labeled cells, NPR-C purification and phosphoamino acid analysis clearly demonstrate that NPR-C exists as a phosphoprotein in RASM cells and that phosphorylation occurs exclusively on serine residues. Transient expression of bovine NPR-C in Cos-P cells of kidney origin confirmed that phosphorylation occurs within the cytoplasmic domain of the receptor. These results provide the first evidence for NPR-C phosphorylation as well as a model for future studies of its role in altering receptor function. |
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Keywords: | natriuretic peptide receptor-C phosphorylation rat aortic smooth muscle cell consensus phosphorylation site |
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