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Characterization of the phosphorylation state of natriuretic peptide receptor-C

Authors
  • Pedro, Liliana1
  • Fenrick, Randy2
  • Marquis, Martin2
  • McNicoll, Normand1
  • De Léan, André1, 2
  • 1 Université de Montréal, Département de Pharmacologie, Montréal, Québec, H3C 3J7, Canada , Montréal
  • 2 Université de Montréal, Département de Biochimie, Montréal, Québec, H3C 3J7, Canada , Montréal
Type
Published Article
Journal
Molecular and Cellular Biochemistry
Publisher
Springer-Verlag
Publication Date
Jan 01, 1998
Volume
178
Issue
1-2
Pages
95–101
Identifiers
DOI: 10.1023/A:1006808604321
Source
Springer Nature
Keywords
License
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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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