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First published online on November 16, 2005
This version published online on January 24, 2006
Endocrine Reviews, doi:10.1210/er.2005-0014
A more recent version of this article appeared on February 1, 2006
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*Compound via MeSH
*Substance via MeSH

Natriuretic Peptides, Their Receptors, and Cyclic Guanosine Monophosphate-Dependent Signaling Functions

Lincoln R. Potter*, Sarah Abbey-Hosch, and Deborah M. Dickey

Department of Biochemistry, Molecular Biology and Biophysics (L.R.P., S.A.-H., D.M.D.), and Department of Pharmacology (L.R.P.), University of Minnesota, Minneapolis, Minnesota 55455

* To whom correspondence should be addressed. E-mail: potter{at}umn.edu.

Natriuretic peptides are a family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. The mammalian members are atrial natriuretic peptide, B-type natriuretic peptide, C-type natriuretic peptide, and possibly osteocrin/musclin. Three single membrane-spanning natriuretic peptide receptors (NPRs) have been identified. Two, NPR-A/GC-A/NPR1 and NPR-B/GC-B/NPR2, are transmembrane guanylyl cyclases, enzymes that catalyze the synthesis of cGMP. One, NPR-C/NPR3, lacks intrinsic enzymatic activity and controls the local concentrations of natriuretic peptides through constitutive receptor-mediated internalization and degradation. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure, whereas homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux. The physiological effects of natriuretic peptides are elicited through three classes of cGMP binding proteins: cGMP-dependent protein kinases, cGMP-regulated phosphodiesterases, and cyclic nucleotide-gated ion channels. In this comprehensive review, the structure, function, regulation, and biological consequences of natriuretic peptides and their associated signaling proteins are described.




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