Immunolocalization of natriuretic peptide receptor B in the rat kidney

Marie Chantal Bonhomme, Kevin L. Grove, Sylvie Caron, Caroline T. Crilley, Gaetan Thibault, Christian F. Deschepper, Raul Garcia

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


The natriuretic peptide receptor (NPR) family consists of three receptor subtypes: two transmembrane forms that contain a guanylyl cyclase intracellular domain (NPR-A and NPR-B), and one truncated form (NPR-C). Because of the lack of specific agonists and antagonists for each receptor subtype and to the difficulty to detect the presence of small quantities of NPR-B by ligand binding studies, polyclonal antibodies against a peptide whose sequence was chosen from a region of the extracellular domain of rat NPR-B that is not homologous to sequences in NPR-A and NPR-C were developed Western blotting with affinity-purified anti-NPR-B (413-426)-Tyr revealed a polypeptide of approximately 120 kD on COS-1 cell membranes transfected with rat NPR-B cDNA. The antibody recognized a second polypeptide, approximately 5 to 10 kD smaller, which probably represents the unglycosylated receptor. Anti-NPR-B (413-426)-Tyr did not show crossreactivity to any other NPR. Western blotting analysis with anti-NPR-B (413-426)-Tyr also identified a protein of appropriate size in renal vascular membranes. These results were supported by immunohistochemistry findings that demonstrated staining for NPR-B on papillary and medullary capillaries, glomeruli, and renal arteries. This study concludes that NPR-B is present in the rat kidney, although it was only detected in vascular structures.

Original languageEnglish (US)
Pages (from-to)1777-1786
Number of pages10
JournalJournal of the American Society of Nephrology
Issue number10
StatePublished - Oct 1998
Externally publishedYes

ASJC Scopus subject areas

  • Nephrology


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