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Natriuretic Peptides and Normal Body Fluid Regulation

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ABSTRACT

Natriuretic peptides are structurally related, functionally diverse hormones. Circulating atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are delivered predominantly by the heart. Two C‐type natriuretic peptides (CNPs) are paracrine messengers, notably in bone, brain, and vessels. Natriuretic peptides act by binding to the extracellular domains of three receptors, NPR‐A, NPR‐B, and NPR‐C of which the first two are guanylate cyclases. NPR‐C is coupled to inhibitory proteins. Atrial wall stress is the major regulator of ANP secretion; however, atrial pressure changes plasma ANP only modestly and transiently, and the relation between plasma ANP and atrial wall tension (or extracellular volume or sodium intake) is weak. Absence and overexpression of ANP‐related genes are associated with modest blood pressure changes. ANP augments vascular permeability and reduces vascular contractility, renin and aldosterone secretion, sympathetic nerve activity, and renal tubular sodium transport. Within the physiological range of plasma ANP, the responses to step‐up changes are unimpressive; in man, the systemic physiological effects include diminution of renin secretion, aldosterone secretion, and cardiac preload. For BNP, the available evidence does not show that cardiac release to the blood is related to sodium homeostasis or body fluid control. CNPs are not circulating hormones, but primarily paracrine messengers important to ossification, nervous system development, and endothelial function. Normally, natriuretic peptides are not powerful natriuretic/diuretic hormones; common conclusions are not consistently supported by hard data. ANP may provide fine‐tuning of reno‐cardiovascular relationships, but seems, together with BNP, primarily involved in the regulation of cardiac performance and remodeling. © 2017 American Physiological Society. Compr Physiol 8:1211‐1249, 2018.

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Figure 1. Figure 1. Schematic overview of transcripts of the three natriuretic peptide genes mainly after (). Blue: Active prototypical peptides consist of the carboxyterminal 28, 32, and 22 peptides of the prohormones for ANP, BNP, and CNP, respectively, with the 17‐member ring as a hallmark. The N‐terminal amino acid of the prohormone is often labeled number 1. For CNP, active ligands include two peptides of 22 and 53 amino acids; blue: CNP‐53, dark blue: CNP‐22. Homologous amino acids are marked in red. SP: signaling peptides; for ANP, BNP, and CNP, these are composed of 25, 26, and 22 amino acids, respectively. For details of nomenclature, see appendix.
Figure 2. Figure 2. Prototypic ligands and receptors of the natriuretic peptide system. AC: adenylate cyclase. GC: guanylate cyclase. Dimerization of NPR‐A and NPR‐B occurs via intracellular domains (not shown). Note that NPR‐C is not GC‐C, see details by Kuhn (). Mainly based on (). With regard to NPR‐C signaling, see ().
Figure 3. Figure 3. Binding of ANP to the extracellular domain of the NPR‐A receptor. (A) Homodimer without ANP. (B) ANP in green. Adapted, with permission, Misono et al. ()
Figure 4. Figure 4. Plasma clearance (metabolic clearance rate, MCR) of ANP as function of plasma ANP concentration in the studies of Table 2 providing the necessary data. Data from 54 series of investigations in 42 studies have been included. Five studies have been omitted as apparent outliers; four of these reported very high levels of plasma ANP (>1700 pg/mL) and one data set gave rise to a very high value of MCR [615 mL (kg min)−1]. MCR averages: Median: 86 mL (kg min)−1, mean: 106 mL (kg min)−1 .The large scatter indicates significant differences in methodology and/or assay performance, but the pattern does not seem to allow further conclusions.


Figure 1. Schematic overview of transcripts of the three natriuretic peptide genes mainly after (). Blue: Active prototypical peptides consist of the carboxyterminal 28, 32, and 22 peptides of the prohormones for ANP, BNP, and CNP, respectively, with the 17‐member ring as a hallmark. The N‐terminal amino acid of the prohormone is often labeled number 1. For CNP, active ligands include two peptides of 22 and 53 amino acids; blue: CNP‐53, dark blue: CNP‐22. Homologous amino acids are marked in red. SP: signaling peptides; for ANP, BNP, and CNP, these are composed of 25, 26, and 22 amino acids, respectively. For details of nomenclature, see appendix.


Figure 2. Prototypic ligands and receptors of the natriuretic peptide system. AC: adenylate cyclase. GC: guanylate cyclase. Dimerization of NPR‐A and NPR‐B occurs via intracellular domains (not shown). Note that NPR‐C is not GC‐C, see details by Kuhn (). Mainly based on (). With regard to NPR‐C signaling, see ().


Figure 3. Binding of ANP to the extracellular domain of the NPR‐A receptor. (A) Homodimer without ANP. (B) ANP in green. Adapted, with permission, Misono et al. ()


Figure 4. Plasma clearance (metabolic clearance rate, MCR) of ANP as function of plasma ANP concentration in the studies of Table 2 providing the necessary data. Data from 54 series of investigations in 42 studies have been included. Five studies have been omitted as apparent outliers; four of these reported very high levels of plasma ANP (>1700 pg/mL) and one data set gave rise to a very high value of MCR [615 mL (kg min)−1]. MCR averages: Median: 86 mL (kg min)−1, mean: 106 mL (kg min)−1 .The large scatter indicates significant differences in methodology and/or assay performance, but the pattern does not seem to allow further conclusions.
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Peter Bie. Natriuretic Peptides and Normal Body Fluid Regulation. Compr Physiol 2018, 8: 1211-1249. doi: 10.1002/cphy.c180002