Disease relevance of BNP

• This study evaluated the effects of acute brain death (BD) on the release of ANP, BNP, big ET-1, and cardiac troponins in an animal model [1].
• Like NO, BNP and CNP facilitate vagal neurotransmission and bradycardia [2].
• Cumulatively, the data suggest that acute hypoxia stimulates cardiac BNP expression [3].
• However, patients with ischemic heart disease also display increased plasma BNP and proBNP concentrations despite preserved cardiac function [3].
• Following de-clamping, BNP was administered to the BNP group (n=10) by an i.v. (intravenous) bolus at 0.3 microg x kg(-1) of body weight x min(-1), followed by an infusion at a rate of 0.015 microg x kg(-1) of body weight x min(-1) for 60 min [4].

High impact information on BNP

• With the use of an indirect immunoperoxidase method, serial sections examined by light microscopy showed foci of multihormonal myocytes containing both ANP and BNP localized in the subendocardium [5].
• Complimentary DNA (cDNA) clones encoding porcine brain natriuretic peptide (BNP) were isolated from a porcine atrial cDNA library [6].
• The identification of these introns suggests that the BNP gene structure differs from the atrial natriuretic peptide gene in the location of intron 2 [6].
• BNP mRNA encodes a propeptide of 131 amino acids, including a signal peptide domain (25 amino acids) and a prohormone domain (106 amino acids) [6].
• In contrast, responses to papaverine and brain natriuretic peptide were unchanged after FPI [7].

Chemical compound and disease context of BNP

• The suppressive effect of aldosterone secretion-inhibitory factor (ASIF) and brain natriuretic peptide (BNP-32) on the basal and ACTH-stimulated cortisol production in a primary culture enriched with guinea pig Zona Fasciculata (ZF) cells was further studied [8].

Biological context of BNP

• This product (BNP') was short-lived; further degradation involved hydrolysis at Ile12-Gly13, Arg8-Leu9, Gly17-Leu18, Val22-Leu23, Arg11-Ile12 and Cys4-Phe5 [9].
• BNP and CNP significantly (P < 0.05) enhanced the heart rate (HR) response to vagal nerve stimulation [2].
• Specific 125I-BNP binding sites were found to be localized in the SFO, an area densely labeled by 125I-alpha-rat atrial natriuretic peptide and 125I-(Sar1,Ile8)-angiotensin II [10].
• By micorosequence analyses of the native high MW BNP as well as its tryptic and chymotryptic peptides, the complete amino acid sequence of the high MW BNP was determined [11].
• This human clone, H1, also contained a sequence homologous to porcine BNP precursor [12].

Anatomical context of BNP

• When the two peptides were incubated with choroid plexus membranes, the products being analysed by h.p.l.c., alpha-hANP was degraded twice as fast as BNP [9].
• We tested both relaxation and cGMP generation by atrial (ANP), brain (BNP), and C-type natriuretic peptide (CNP) in oxytocin-stimulated myometrium from near-term pregnant guinea pigs to investigate the ability and mechanism of natriuretic peptides to inhibit myometrial contractility [13].
• Biochemical and cytochemical analyses of BNP-stimulated guanylate cyclase in frog choroid plexus [14].
• Ultracytochemical tests for GC show that BNP notably increases the enzymatic reaction product along the apical surfaces of the epithelial cells [14].
• Guinea pig caecal circular smooth muscle cells were used to determine whether brain natriuretic peptide (BNP) can inhibit the contractile response produced by cholecystokinin-octapeptide (CCK-8) [15].

Associations of BNP with chemical compounds

• The results were compared with the effects of atrial (ANP) and brain (BNP) natriuretic peptides [16].
• Anantin, a competitive blocker of the guanylate cyclase A receptor, significantly reduced the increase in cGMP produced by ANP and BNP, but had no effect on relaxation induced by either peptide [13].
• We showed that the rank order of inhibitory potencies, which were mediated by cyclic guanosine 3',5'-monophosphate, was BNP > or = ANP > or = CNP [17].
• Acquisition of these present findings enhances our knowledge of the physiology of BNP, atrial natriuretic peptides and angiotensin II system in the SFO [10].
• The amino acid sequence determined for the peptide shows remarkable similarity to those of ANP and BNP, especially in the 17-residue sequences flanked by two cysteine residues [18].

Other interactions of BNP

• INTRODUCTION: Atrium and B-type natriuretic peptides (ANP and BNP) and big endothelin (ET)-1 are markers for severity of heart failure and may be used in the quality assessment of donor hearts [1].
• BNP inhibited the contractile response produced by CCK-8 in a dose-response manner, with an IC50 value of 8.5 nM, and stimulated the production of cAMP [15].
• Captopril had no effect and, indeed, no hydrolysis of BNP-26 by peptidyl dipeptidase A (angiotensin-converting enzyme) was observed even after prolonged incubation with the purified enzyme [9].

Analytical, diagnostic and therapeutic context of BNP

• A partial cDNA clone representing processed BNP mRNA was prepared by polymerase chain reaction [6].
• Cloning and sequence analysis of cDNA encoding a precursor for porcine brain natriuretic peptide [19].
• At the electron microscopic level, double immunocytochemistry using a two-face immunogold-staining method revealed two types of granules: Type 1 is a monohormonal granule containing ANP alone, and type 2 is a multihormonal granule containing both ANP and BNP [5].
• In the control group, the BNP level was higher than in the BD group and decreased over time (P =0.016) [1].
• A highly specific and sensitive radioimmunoassay (RIA) for a novel porcine brain natriuretic peptide (BNP) has been established to elucidate whether BNP-like immunoreactivity (LI) is present in human plasma [20].

References