HeLa cells contain the atrial natriuretic peptide receptor with guanylate cyclase activity

• Published in: Biochemical and biophysical research communications Vol. 164; no. 2; pp. 671 - 677
• Main Authors: Watt, Valerie M., Yip, Cecil C.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.10.1989; Elsevier
• Subjects: Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Atrial Natriuretic Factor - metabolism; Binding, Competitive; Biological and medical sciences; Cell Line; Cyclic GMP - metabolism; Fundamental and applied biological sciences. Psychology; Guanylate Cyclase - isolation & purification; Guanylate Cyclase - metabolism; HeLa cells; HeLa Cells - metabolism; Humans; Kinetics; Molecular Weight; Proteins; Receptors, Atrial Natriuretic Factor; Receptors, Cell Surface - isolation & purification; Receptors, Cell Surface - metabolism; PBS; SDS-PAGE; ANP; HBSS; HG-DMEM; Human; Cell culture; Ligand binding; Radiolabelling; Peptide hormone; Atrial natriuretic peptide; Photoaffinity labelling; Guanylate cyclase; Hela cell line; Natriuretic hormone; Enzymatic activity; Models; Hormonal receptor
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(89)91512-X

Receptors for atrial natriuretic peptide (ANP) are heterogeneous: an ≈140-kDa receptor exhibits ANP-stimulated guanylate cyclase activity whereas an ≈65-kDa receptor is thought to act only as a clearancestorage protein. We have used photoaffinity labeling techniques to show that the human cell line, HeLa, contains predominantly the ≈140-kDa ANP receptor. In contrast, several other cell lines contain primarily the ≈65-kDa receptor. In HeLa cells, ANP bound specifically to high affinity binding sites (Kd≈2 nM) and stimulated a rapid, dose-dependent accumulation of cGMP. These cell lines can thus provide useful models to study the multiple mechanisms of ANP action.