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Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases

Nature volume 341, pages 68–72 (1989)Cite this article

Abstract

ALPHA atrial natriuretic peptide (α-ANP) and brain natriuretic peptide are homologous polypeptide hormones involved in the regulation of fluid and electrolyte homeostasis1,2. These two natriuretic peptides apparently share common receptors and stimulate the intracellular production of cyclic GMP as a second messenger1. Molecular cloning has defined two types of natriuretic peptide receptors: the ANP-C receptor of relative molecular mass (Mr) 60–70,000 (60–70 K), which is not coupled to cGMP production and may function in the clearance of ANP (refs 3,4) and the ANP-A receptor of Mr 120–140 K, which is a membrane form of guanylate cyclase in which ligand binding to the extracellular domain activates the cytoplasmic domain of the enzyme5,6. Here we report the cloning and expression of a second human natriuretic peptide-receptor guanylate cyclase, the ANP-B receptor. The ANP-B receptor is preferentially activated by porcine brain natriuretic peptide rather than human α-ANP, whereas the ANP-A receptor responds similarly to both natriuretic peptides. These observations may have important implications for our understanding of the central and peripheral control of cardiovascular homeostasis.

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Affiliations

  1. Department of Molecular Biology, Genentech Inc., 460 Point San Bruno Boulevard, South San Francisco, California, 94080, USA

    Ming-shi Chang, David G. Lowe, Martyn Lewis, Renate Hellmiss, Ellson Chen & David V. Goeddel

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  1. Ming-shi Chang
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  2. David G. Lowe
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  3. Martyn Lewis
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  4. Renate Hellmiss
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  5. Ellson Chen
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  6. David V. Goeddel
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Chang, Ms., Lowe, D., Lewis, M. et al. Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases. Nature 341, 68–72 (1989). https://doi.org/10.1038/341068a0

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