Disease relevance of NPPA

• In vivo gene transfer of ANP may provide us with the opportunity of gene therapy for vascular diseases in which the abnormalities are vasoconstriction and pathological growth [1].
• By contrast, calcium ionophore or atrial natriuretic peptide caused elevations of cGMP that were not affected by TEA or pertussis toxin [2].
• BACKGROUND: Atrial natriuretic peptide, brain natriuretic peptide and C-type natriuretic peptide belong to a family of hormones that have natriuretic and vasodepressor activity and may play a pathophysiologic role in hypertension, heart failure and renal failure [3].
• Relaxations induced by SIN-1, but not by ANP were increased (P < 0.001) under hypoxia and decreased (P = 0.002) under hyperoxia [4].
• This PDE5-dependent ANP resistance may represent an important contributor to the sodium retention of liver disease [5].

High impact information on NPPA

• This hormone, described in 1981 as atrial natriuretic factor (ANF), is diuretic (natriuretic), hypotensive, and has an inhibitory effect on renin and aldosterone secretion [6].
• Our results indicate that ANP and BNP can stimulate CNP production through a guanylate cyclase receptor on endothelial cells [7].
• The enhanced production and secretion of CNP, caused by either ANP or BNP, was significantly prevented by LY 83583, an inhibitor of cGMP generation, and was also attenuated by KT 5823, an inhibitor of cGMP-dependent protein kinase [7].
• Transfection of the ANP vector decreased DNA synthesis in VSMC under basal and angiotensin II-stimulated conditions [1].
• Autocrine and paracrine effects of atrial natriuretic peptide gene transfer on vascular smooth muscle and endothelial cellular growth [1].

Chemical compound and disease context of NPPA

• Levels of pertussis toxin sufficient to inhibit subsequent in vitro ribosylation did not significantly alter the ANP effect on aldosterone production, although a partial reduction in the ANP effect on cAMP levels was observed.(ABSTRACT TRUNCATED AT 400 WORDS)[8]
• Effect of the ANF analog A68828 in cisplatin-induced acute renal failure [9].
• Pertussis toxin (PTX; 200 ng/ml for 18 h) augmented the relaxation and accumulation of guanosine 3',5'-cyclic monophosphate produced by ANP [10].
• The inhibitory effect of ANP on Tg mRNA level was reverted in the presence of pertussis toxin, an inhibitor of the G(i)-protein-mediated reduction of the adenylate cyclase activity [11].
• Original studies with rat adrenocortical carcinoma identified a 180 kDa cell-surface protein which contained both guanylate cyclase and atrial natriuretic factor (ANF) receptor, representing a potentially new type of bifunctional receptor protein [12].

Biological context of NPPA

• Deciphering vascular endothelial cell growth factor/vascular permeability factor signaling to vascular permeability. Inhibition by atrial natriuretic peptide [13].
• Examination of the pre-proANP amino acid sequence derived from the bovine gene with those from rat, mouse and human, indicates a high degree of sequence homology in both the amino-terminal and biologically-active carboxy-terminal ANP region [14].
• The bovine-ANP coding sequences are located on three exons which are interrupted by two intervening sequences [14].
• Finally, we examined the autocrine effect of direct transfection of ANP vector into VSMC [1].
• Using primary cardiocyte cultures from neonate rat hearts, an alpha 1-adrenergic regulatory sequence has been identified in the 5' flanking region of the ANF gene [15].

Anatomical context of NPPA

• The monitoring of the activity along the purification steps was performed with a radio-receptor assay using bovine adrenal cortex membranes sites and 125I ANF [16].
• We report the purification and the sequence determination of bovine atrial natriuretic factor (ANF) in acid extracts of bovine atrial appendages [16].
• C-type natriuretic peptide (CNP), the third member of the natriuretic peptide family, is thus far known to be distributed mainly in the central nervous system and is considered to act as a neuropeptide, in contrast to atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP), which act as cardiac hormones [17].
• A receptor for atrial natriuretic peptide (ANP) was purified 2700-fold, to apparent homogeneity, from cultured bovine aortic smooth muscle cells by affinity chromatography [18].
• The coexistence of ANF and angiotensin II receptors on this cerebrovascular tissue suggests that the two circulating peptides may act as mutual antagonists in the regulation of brain microcirculation and/or blood-brain barrier function [19].

Associations of NPPA with chemical compounds

• Subsequent purification steps by reverse phase mode on Ultrapore RPSC, Vydac TP 218 and uBondapak using acetonitrile gradients led to the obtention of a pure fraction which amino acid sequence was identical to that for human ANF [16].
• Addition of conditioned medium from endothelial cells transfected with ANP vector to nontransfected endothelial cells resulted in the significant increase in cyclic GMP [1].
• The native ANP receptor has a molecular weight of 125,000 as determined by both metrizamide gradient centrifugation and nonreducing NaDodSO4/polyacrylamide gel electrophoresis [18].
• Moreover, the kinetics of atrial natriuretic peptide-stimulated PDE2 activity (measured as decline of cAMP) are much faster than the speed of ACTH and isoprenaline-induced cAMP-synthesis (measured as cAMP accumulation) in the cells, revealing high catalytic activity and fast action of PDEs in regulating cAMP signaling in a physiological system [20].
• Increases in aldosterone production elicited by three cell-permeable cAMP derivatives (8-bromo-cAMP, 8-p-chlorophenylthio-cAMP, and N6-2'-O-dibutyryl-cAMP) were antagonized by ANP, indicating a site of action distal to adenylate cyclase for this hormone [8].

Regulatory relationships of NPPA

• Atrial natriuretic peptide inhibits iodide uptake and thyroglobulin messenger ribonucleic acid expression in cultured bovine thyroid follicles [11].
• Atrial natriuretic peptide inhibits the production and secretion of endothelin from cultured endothelial cells. Mediation through the C receptor [21].
• Atrial natriuretic peptide inhibits calcium-induced steroidogenic acute regulatory protein gene transcription in adrenal glomerulosa cells [22].
• 4. Phosphoramidon potentiated atrial natriuretic peptide-induced relaxation of methacholine-induced tone and the ability of atrial natriuretic peptide to protect against methacholine-induced contraction [23].
• Atrial natriuretic peptide reduces cyclic AMP by activating cyclic GMP-stimulated phosphodiesterase in vascular endothelial cells [24].

Other interactions of NPPA

• A novel form of type C atrial natriuretic peptide receptor (ANP-C) was identified, characterized, and shown to be a product of alternative RNA splicing [25].
• An adrenal cGMP-stimulated phosphodiesterase (cGS-PDE) has been shown to mediate atrial natriuretic peptide (ANP)-induced reductions in aldosterone secretion and cAMP levels in primary bovine glomerulosa cells [8].
• Characterization by affinity cross-linking of a receptor for atrial natriuretic peptide in cultured human thyroid cells associated with reductions in both adenosine 3',5'-monophosphate production and thyroglobulin secretion [26].
• STUDY OBJECTIVE--The aim of the study was to investigate plasma concentrations of atrial natriuretic peptide, aldosterone, and renin during experimentally induced acute central venous congestion [27].
• Atrial natriuretic peptide in bovine corpus luteum [28].

Analytical, diagnostic and therapeutic context of NPPA

• The isolation and sequence analysis of the gene encoding the bovine atrial natriuretic peptide (ANP) precursor is described [14].
• Bovine ANF was separated by carboxymethyl agarose gel chromatography from catecholamines and major protein contaminants [16].
• Coculture of ANP-transfected endothelial cells with quiescent VSMC showed that released ANP from endothelial cells inhibited DNA synthesis in VSMC [1].
• Affinity cross-linking of 125I-ANF to its binding sites in zona glomerulosa membranes and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that one single band with apparent Mr 130,000 was specifically labeled [29].
• With reversed-phase HPLC, a major immunoreactive peak of CNP or ANP was observed at the elution time corresponding with synthetic CNP(1-53) or atriopeptin III (APIII), respectively [30].

References