Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry

Inooka, Hiroshi; Kikuchi, Takashi; Endo, Satoshi; Ishibashi, Yoshihiro; Wakimasu, Mitsuhiro; Mizuta, Eiji

doi:10.1111/j.1432-1033.1990.tb19313.x

Cited by 18 publications

(24 citation statements)

References 37 publications

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“…Overall the peptide appears to be flexible, with the possibility of some P-type structure near the C terminus. Some of the assignments and deduced structural features in the current study differ from those in a recent report by Inooka et al [Inooka, H., Kikuchi, T., Endo, S., Ishibashi, Y., Wakimasu, M. and Mizuta, E. (1990) Eur. J. Biochem.…”

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confidence: 56%

The conformation of porcine‐brain natriuretic peptide by two‐dimensional NMR spectroscopy

Craik¹,

Munro²,

Nielsen³

et al. 1991

European Journal of Biochemistry

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Two-dimensional (2D) 'H-NMR spectra of porcine-brain natriuretic peptide (pBNP) have been recorded at 300 MHz and 400 MHz. Peak assignments have been made and the combined information from chemical shifts, coupling constants, temperature coefficients and NOES have been used to determine the conformational properties of pBNP in (C2H3)2S0. Overall the peptide appears to be flexible, with the possibility of some P-type structure near the C terminus. Some of the assignments and deduced structural features in the current study differ from those in a recent report by Inooka et al. [Inooka, H., Kikuchi, T., Endo, S., Ishibashi, Y., Wakimasu, M. and Mizuta, E. (1990) Eur. J. Biochem. 193,127-1341 which may indicate the sensitivity of the structure of this peptide to differences in solution conditions. Brain natriuretic peptide (BNP) is a novel peptide originally isolated from porcine brain [l]. It consists of 26 amino acid residues with the sequence shown in Fig. 1. An internal disulfide bond exists between the cysteine residues at positions 4 and 20, which gives rise to the expectation that this relatively small peptide may have a well-defined structure in solution.BNP closely resembles and elicits pharmacological responses very similar to atrial natriuretic peptide (ANP). These effects include natriuretic/diuretic, hypotensive and relaxant responses. It has therefore been suggested [l] that physiological functions such as water intake and salt appetite, which have previously been thought to be controlled by ANP, may also be regulated by BNP. BNP has been found to have a stronger inhibitory effect on cardiac function than ANP and like ANP, may play an important role in the pathogenesis of cardiovascular diseases [2]. Autoradiographic studies [3] have shown that BNP and ANP share binding sites in the heart and kidney. Radioimmunoassay studies [4] indicate that BNP is also synthesized in the heart and secreted from there into the circulatory system in a manner similar to ANP.A 2D NMR study [5] of a-human ANP concluded that it had a defined conformation in (C2H&30, although convergence amongst the six best conformers was not good, with a root-mean-square distance of 0.47 nm between superimposed backbone atoms. NMR studies [6 -91 of other closely related ANP analogues found no well-defined structures in solution.In view of the physiological importance of this recently discovered peptide, we have undertaken a 'H-NMR study of Abbreviations. BNP, brain natriuretic peptide; pBNP, porcine BNP; ANP, atrial natriuretic peptide; DQF-COSY, double-quantumfiltered proton-correlated spectroscopy; NOESY, nuclear Overhauser enhancement spectroscopy; HOHAHA, homonuclear HartmannHahn spectroscopy; 2D, two dimensional. pBNP in (C2H3)2S0 using 2D techniques. While this manuscript was in preparation, a report [lo] appeared on the NMR assignment and conformation of pBNP in (C2H&SO-There are a number of assignments in that study which are markedly different to our own and these differences will be discussed in detail in the results section. ...

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contrasting

confidence: 56%

The conformation of porcine‐brain natriuretic peptide by two‐dimensional NMR spectroscopy

Craik¹,

Munro²,

Nielsen³

et al. 1991

European Journal of Biochemistry

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“…NMR studies [12,13] have shown that the conformations of residues 1-16 of Big ET-1 are very similar to those of the same residues in ET-1. However, the NMR studies have been unable to define accurately a structure for the part of the Big ET-1 molecule beyond residue 16, so the nature of the all-important C-terminal extension remains unknown.…”

Section: Discussionmentioning

confidence: 99%

A molecular model for human Big‐Endothelin‐1 (Big ET‐1)

et al. 1996

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“…Inooka et al (1990) published a solution structure analysis of porcine BNP and Kobayashi et al (1988) that of human ANP. We have investigated 339 Fig.…”

Section: Structural Properties Of Natriuretic Peptidesmentioning

confidence: 99%

The endocrine heart and natriuretic peptides: histochemistry, cell biology, and functional aspects of the renal urodilatin system

Forssmann

Richter

Meyer

1998

Histochemistry and Cell Biology

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This review focuses on some selected aspects of the endocrine heart and natriuretic peptides. The endocrine heart is composed of specific myoendocrine cells of the cardiac atria. The myoendocrine cells synthesize and secrete the natriuretic peptide hormones which exhibit natriuretic, diuretic, and vasorelaxant properties. Immunohistochemical analyses show that natriuretic peptides of the A-type and B-type are localized not only in the specific granules of these myoendocrine cells but also in many other organs including the brain, adrenal medulla, and kidney. Also, their receptors are detected in many organs showing the multiple functions of these regulatory peptides. Of the members of the natriuretic peptide family, ANP (ANP for atrial natriuretic peptide; also denominated cardiodilatin, CDD), brain natriuretic peptide (BNP), C-type natriuretic peptide (CNP), and the A-type, including its renal form, urodilatin, are emphasized in this review. Urodilatin is localized in the kidney, differentially processed, and secreted into the urine. The intrarenal synthesis and secretion is the basis for a paracrine system regulating water and sodium reabsorption at the level of the collecting duct. CDD/ANP-1-126, cleaved from a precursor of 126 amino acids in the heart to a 28-amino acid-containing circulating molecular form (CDD/ANP-99-126), and urodilatin (CDD/ANP-95-126) share similar biochemical features and biological functions, but urodilatin may be more involved in the regulation of body fluid volume and water-electrolyte excretion, while circulating CDD/ANP-99-126 is responsible for blood pressure regulation. The physiological and pharmacological properties of these peptides have great clinical impact, and as a consequence urodilatin is involved in drug development for the treatment of acute renal failure, cardiomyopathia, and acute asthma.

show abstract

Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry

Cited by 18 publications

References 37 publications

The conformation of porcine‐brain natriuretic peptide by two‐dimensional NMR spectroscopy

The conformation of porcine‐brain natriuretic peptide by two‐dimensional NMR spectroscopy

A molecular model for human Big‐Endothelin‐1 (Big ET‐1)

The endocrine heart and natriuretic peptides: histochemistry, cell biology, and functional aspects of the renal urodilatin system

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