C-ANP

In addition to the structures in Figures 8.30 and 8.36, three more crystal structures of the Fi-ATPase have been determined by the Walker group. The first of the three involve the occupancy states of ATP(A), ATP(B), ATP(C), ADP(D), P04(E), and ATP(F) for the protein structure listed in the Protein Data Bank as Structure File 1H8H. The second of the three involve the occupancy states of ANP(A), ANP(B), ANP(C), ADP(D), P04(E), and ANP(F) where PNP may also be represented as AMPPNP, that is, a nitrogen replaces the bridge oxygen of ATP between the P-and y-phosphates this structure, shown in Figure 8.37, is listed in the Protein Data Bank as Structure File lElQ. The third of the three additional structures involves occupancy states of ANP(A), ANP(B), ANP(C), ANP(D), empty(E), and ANP(F) and is listed in the Protein Data Bank as Structure File In each case the hydrophobic side of the y-rotor faces the occupancy state of chain E. 

Atrial Natriuretic Peptide, a-Atrial natriuretic peptide [85637-73-6] (ANP) (55), also known as atrial natriuretic factor (ANF), brain natriuretic peptide (BNP) (56), and type C natriuretic peptide (CNP) (57) are members of the ANP family (28). These atrial peptides arise from a common 128 amino acid precursor where the active form of ANP is the 28 amino acid peptide at the C terminus. 

At low (1—10 nAf) concentrations ANP activates ANP whereas ANPg appears to be the physiological receptor for CNP. ANP and BNP are inactive at the latter subtype except at high micromolar concentrations. AP 811 [124833 5-OJ C gHggN 20g (58) is a selective ANP ligand. (L-a-Aminosuberic is an ANP antagonist. 

The acyclic nucleoside phosphonates (ANPs) can be considered as nucleotide rather than nucleoside analogues, in that, besides the purine or pyrimidine base, they contain an (acyclic) sugar moiety to which a phosphonate is attached. In these nucleotide analogues (Fig. 2), the phosphoric ester grouping (= P-O---C-----) is... 

After approximately 90 min of anoxia, the induced synthesis of an additional group of c. 20 polypeptides is first detected. This group of 20 anaerobic polypeptides (ANPs) represents more than 70% of the total labelled amino acid incorporation after five hours of anaerobiosis (Fig. 3). By this time the synthesis of the TPs is at a minimal level however, these polypeptides accumulate to a high level during early anaerobiosis and have been shown by pulse-chase experiments to be very stable. The synthesis of... 

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). 

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. 

Natriuretic peptides (NPs) are a group of peptide hormones in animals that are critically involved in salt and water homeostasis (for review see [5]). NPs include atrial NP (ANP), brain NP (BNB), C-type NP (CNP), and urodilatin all of which are synthesized as larger precursor proteins. In... 

Antihuman atrial natriuretic peptide (ANP) in serum 1997 C Factor (time) 10 (IPCR 5 hours, IRMA 2-3 days) Numata et al. [99]... 

Hiner ANP, Hemandez-Rtuz J, Amao MB et al (1996) A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C. Biotechnol Bioeng 50 655-662... 

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