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
Correspondence: Address all correspondence and requests for reprints to: Lincoln R. Potter, Department of Biochemistry, Molecular Biology, and Biophysics, 6-155 Jackson Hall, 321 Church Street SE, University of Minnesota, Minneapolis, Minnesota 55455. E-mail: potter{at}umn.edu
Natriuretic peptides are a family of structurally related butgenetically distinct hormones/paracrine factors that regulateblood volume, blood pressure, ventricular hypertrophy, pulmonaryhypertension, fat metabolism, and long bone growth. The mammalianmembers 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 thesynthesis of cGMP. One, NPR-C/NPR3, lacks intrinsic enzymaticactivity and controls the local concentrations of natriureticpeptides through constitutive receptor-mediated internalizationand degradation. Single allele-inactivating mutations in thepromoter of human NPR-A are associated with hypertension andheart failure, whereas homozygous inactivating mutations inhuman NPR-B cause a form of short-limbed dwarfism known as acromesomelicdysplasia type Maroteaux. The physiological effects of natriureticpeptides are elicited through three classes of cGMP bindingproteins: cGMP-dependent protein kinases, cGMP-regulated phosphodiesterases,and cyclic nucleotide-gated ion channels. In this comprehensivereview, the structure, function, regulation, and biologicalconsequences of natriuretic peptides and their associated signalingproteins are described.
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