C-type natriuretic peptide

Atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and C-type natriuretic peptide (CNP) are members of a family of so-called natriuretic peptides, synthesized predominantly in the cardiac atrium, ventricle, and vascular endothelial cells, respectively (G13, Y2). ANP is a 28-amino-acid polypeptide hormone released into the circulation in response to atrial stretch (L3). ANP acts (Fig. 8) on the kidney to increase sodium excretion and glomerular filtration rate (GFR), to antagonize renal vasoconstriction, and to inhibit renin secretion (Ml). In the cardiovascular system, ANP antagonizes vasoconstriction and shifts fluid from the intravascular to the interstitial compartment (G14). In the adrenal cortex, ANP is a powerful inhibitor of aldosterone synthesis (E6, N3). At the hypothalamic level, ANP inhibits vasopressin secretion (S3). It has been shown that some of the effects of ANP are mediated via a newly discovered hormone, called adreno-medullin, controlling fluid and electrolyte homeostasis (S8). The diuretic and blood pressure-lowering effect of ANP may be partially due to adrenomedullin (V5). 

CSTR reactor system, 23 396. See also Continuous- stirred tank reactor (CSTR) anionic polymerization C-toxiferine, 2 74, 99 C-type inks, 14 324, 326 C-type natriuretic peptide (CNP), 5 186-187... 

Natriuretic peptides are naturally occurring substances in the body that oppose the activity of the renin-angiotensin system. The natriuretic peptide family consists of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and C-type natriuretic peptide (CNP). All three natriuretic peptides are synthesized from cleavage of a larger precursor polypeptide. In the ventricles and brain, the synthesis of BNP predominates ANP is synthesized by cardiac myocytes predominately in the atria and CNP is synthesized in the brain, blood vessels, and kidney. 

ANP now belongs to a family of natrinreteic peptides that also includes BNP (brain natrinretic peptide) and CNP (C-type natriuretic peptide). BNP and CNP have different N- and C-termini to ANP. CNP has a shorter N-terminal than either ANP or BNP. CNP has less natriuretic and diuretic activity than ANP or BNP. 

The atria and other tissues of mammals contain a family of peptides with natriuretic, diuretic, vasorelaxant, and other properties. The family includes atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and C-type natriuretic peptide (CNP). The peptides share a common 17-amino-acid disulfide ring with variable C- and N-terminals (Figure 17-5). A fourth peptide, urodilatin, has the same structure as ANP with an extension of four amino acids at the N-terminal. 

Structures of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and C-type natriuretic peptide (CNP). Sequences common to the peptides are indicated in green. 

Sudoh T, Minamino N, Kangawa K, Matsuo H (1990) C-type natriuretic peptide (CNP) a new member of natriuretic peptide family identified in porcine brain. Biochem Biophys Res Commun 168 863-70... 

The authors proposed that increased GABA activity had inhibited natriuresis by altering the action of nitric oxide in the kidneys or by inhibiting the central production of C-type natriuretic peptide. 

CNP atrial natriuretic peptides C-type natriuretic peptide. 

C-type natriuretic peptide (CNP) the newest member of the natriuretic peptide family, was first isolated from porcine brain, and later found in other mammals and nonmammals. It is processed from a pre-pro-CNP molecule, which gives rise to CNP-22 and its N-terminally elongated form. CNP-53. The CNP s share considerable sequence homology with atrial NATRIURETIC PEPTIDES (ANP) and brain natriuretic peptides (BNP). CNP s are atrial NATRIURETIC PEPTIDE RECEPTOR AGONISTS but are more active at the type-B subtype, whereas ANP s are more active at the type-A subtype. 

Natriuretic peptides (NP) are secreted to regulate fluid volume, blood pressure, and electrolyte balance. They have activity in both the central and peripheral nervous systems. ANP was the first described in 1981. BNP was discovered 7 years later in the porcine brain, thus the name. However, in humans, while produced in the brain, the main source of circulatory BNP is the heart ventricles. Other members of the NP family include C-type natriuretic peptide (CNP) and urodilatin. Although these two hormones are not produced by myocardium, they are released with ANP and BNP in patients with volume overload, hypertension, and hyponatremia. 

Kalra PR, Clague JR, Bolger AP, Anker SD, Poole-Wilson PA, Struthers AD, et al. Myocardial production of C-type natriuretic peptide in chronic heart failure. Circulation 2003 107 571-3. 

The natriuretic peptide family has three members, atrial natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP). ANP is stored mainly in the right atrium, whereas BNP is found mainly in the ventricles. Both are released in response to pressure or volume overload. CNP is found mainly in the brain and has very low plasma concentrations. ANP and BNP plasma concentrations are elevated in patients with heart failure and are thought to balance the effects of the RAA system by causing natriuresis, diuresis, vasodilation, decreased aldosterone release, decreased hypertrophy, and inhibition of the SNS and the RAA system. 

ACC American College of Cardiology ACE angiotensin-converting enzyme AHA American Heart Association ANP atrial natriuretic peptide ARB angiotensin receptor blocker AVP arginine vasopressin BNP B-type natriuretic peptide cAMP cyclic adenosine monophosphate CNP C-type natriuretic peptide CO cardiac output... 

NESIRITIDE Nesiritide (natrecor), a recombinant form of human brain natriuretic peptide (BNP), is FDA-approved for treatment of dyspnea due to congestive heart failure. The natriuretic peptides—atrial natriuretic peptide (ANP), BNP, and C-type natriuretic peptide—are a family of endogenous hormones that possess potent natriuretic, diuretic, and vasodilator properties. BNP is secreted by ventricular cardiac myocytes in response to stretch circulating levels of BNP correlate with the severity of heart failure. In the setting of heart failure, the effects of BNP counteract the effects of Angll and NE by producing vasodilation, natriuresis, and diuresis. 

A. Source and Disposition Atrial natriuretic peptide (ANP also known as atrial natriuretic factor [ANF]) is synthesized and stored in the cardiac atria of mammals. Atrial natriuretic peptide is released from the atria in response to distension of the chambers. Two similar peptides, brain natriuretic peptide (BNP) and C-type natriuretic peptide (CNP), have been isolated from brain, heart, and other tissues. 

Ornithorhynchus venom C-type natriuretic peptide B (OvCNPa), a biologically adive peptide found in platypus venom. OvCNPa and its D-amino-acid-containing isomer (D-Leu ), OvCNPb, cause rat uterine smooth musde relaxation, edema and mast cdl histamine release [G. M. de Plater et al., Toxicol. Endocrinol. 1998, 120, 99 Toodcon 1998, 36, 847 A. M. Torres et al., Toodcon 2002, 40, 711 FEES Lett. 2002, 524, 172]. 

Manipulating cychc guanosine monophosphate levels by sodium nitroprusside (10 M), atrial natriuretic peptide (10 M), brain natriuretic peptide (10 M), and C-type natriuretic peptide (10 M) aU had no effect on short-circuit current measurements when added both the serosal and mucosal surfaces of ovine tracheal epithelia mounted in modified Ussing chambers (Range et al. 1997). 10 M 3-Isobutyl-1-methylxanthine (a non-specific phosphodiesterase inhibitor) when added to the mucosal surface resulted in a mean reduction in short-circuit current of 4.3 [lA. cm" (8.9 % of baseline). 

Preincubation of bovine chromaffin cells with C-type natriuretic peptide, which increased cGMP levels and activated cGMP-dependent protein kinase, or with cGPM-permeant analogue (which also activates cGMP-dependent protein kinase), in the presence of a broad-spectrum phosphodiesterase inhibitor, resulted in a decrease in subsequent sodium nitroprusside -dependent cGMP elevations (Ferrero et al. 2000). 

Several V-terminally truncated C-type natriuretic peptides were isolated from the venom of the habu snake [1297]. Separation of these components was achieved on a C 8 column (A = 214nm) using a 30-min 100/0 ->40/60 water (0.1% TEA)/ acetonitrile gradient. Peak shapes were excellent. 

C-type natriuretic peptide from platypus Ornithorhyr)chus anatinus venom [451]... 

---