Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

Hirata, Yukio; Yoshimi, Hiroki; Takata, Satoru; Matsubara, Hiroaki; Takagi, Yasuyuki; Iida, Takatoshi; Chino, Naoyoshi; Watanabe, Takushi X.; Kimura, Terutoshi; Sakakibara, Shumpei

doi:10.1016/0014-5793(87)80255-7

Cited by 8 publications

(6 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, a dicarba analog β ‐ANP acts as antagonist against α ‐ANP and inhibits the α ‐ANP‐induced cyclic guanosine monophosphate production in a dose‐dependent manner . These observations are consistent with the lower affinity of β ‐ANP to NPR‐A; the maximal binding capacity of β ‐ANP to the receptor is one‐half that of α ‐ANP .…”

Section: Introductionsupporting

confidence: 68%

Three molecular forms of atrial natriuretic peptides: quantitative analysis and biological characterization

Nagai‐Okatani

Kangawa

Minamino

2017

Journal of Peptide Science

View full text Add to dashboard Cite

Atrial natriuretic peptide (ANP) is primarily produced in the heart tissue and plays a pivotal role in maintaining cardiovascular homeostasis in endocrine and autocrine/paracrine systems and has clinical applications as a biomarker and a therapeutic agent for cardiac diseases. ANP is synthesized by atrial cardiomyocytes as a preprohormone that is processed by a signal peptidase and stored in secretory granules as a prohormone. Subsequent proteolytic processing of ANP by corin during the secretion process results in a bioactive form consisting of 28 amino acid residues. Mechanical stretch of the atrial wall and multiple humoral factors directly stimulates the transcription and secretion of ANP. Secreted ANP elicits natriuretic and diuretic effects via cyclic guanosine monophosphate produced through binding to the guanylyl cyclase-A/natriuretic peptide receptor-A. Circulating ANP is subjected to rapid clearance by a natriuretic peptide receptor-C-mediated mechanism and proteolytic degradation by neutral endopeptidase. In humans, ANP is present as three endogenous molecular forms: bioactive α-ANP, a homodimer of α-ANP designated as β-ANP, and an ANP precursor designated as proANP (also referred to as γ-ANP). The proANP and especially β-ANP, as minor forms in circulation, are notably increased in patients with cardiac diseases, suggesting the utility of monitoring the pathophysiological conditions that result in abnormal proANP processing that cannot be monitored by inactive N-terminal proANP-related fragments. Emerging plate-based sandwich immunoassays for individual quantitation of the three ANP forms enables evaluation of diagnostic implications and net ANP bioactivity. This new tool may provide further understanding in the pathophysiology of cardiac diseases. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

show abstract

Section: Introductionsupporting

confidence: 68%

Three molecular forms of atrial natriuretic peptides: quantitative analysis and biological characterization

Nagai‐Okatani

Kangawa

Minamino

2017

Journal of Peptide Science

View full text Add to dashboard Cite

show abstract

“…1). In contrast to&ANP, which tends to be converted into cr-ANP when incubated with human plasma [5] or cultured rat VSMC [6], analog III does not under-go such conversion under the usual physiological conditions because of the presence of an Asu residue in the molecule.…”

Section: Discussionmentioning

confidence: 99%

“…&ANP is also known to be converted into cu-ANP when incubated with human plasma [5] or rat cultured vascular smooth-muscle cells (VSMC) [6]. In view of these facts, Itoh et al [5] suggested that the slow onset and long-acting property of P-ANP was a consequence of its slow conversion into a-ANP.…”

mentioning

confidence: 99%

A dicarba analog of β‐atrial natriuretic peptide (β‐ANP) inhibits guanosine 3′,5′‐cyclic monophosphate production induced by α‐ANP in cultured rat vascular smooth muscle cells

et al. 1989

View full text Add to dashboard Cite

The synthesis and biological properties are described of [As~'~~']-/l-ANP-(7-28) (Asu, L-a-aminosuberic acid), a dicarba analog of p-atria1 natriuretic peptide (8-ANP, an antiparallel dimer of human a-ANP with the chains linked by 7-23' and 7-23 disulfide bonds). This Asu-analog (referred to as analog III) displaced 12SI-a-ANP specifically bound to cultured rat vascular smooth muscle cells (VSMC) with an apparent Ki of 2.1 x 10-s M, but did not stimulate formation of intracellular cGMP at 10-8-10-5 M. Analog III inhibited the a-ANP-stimulated cGMP production in VSMC competitively with a pA, value of 7.45 and behaved as an antagonist of a-ANP in rat aorta smooth muscle relaxation. In addition, /I-ANP was also shown to inhibit the a-ANP-induced cGMP production in a dose-dependent manner. The mechanism of action of /I-ANP is also discussed.Atria1 natriuretic peptide analog; Atria1 natriuretic peptide receptor antagonist; Receptor binding; cyclic GMP production; Vasorelaxation; (Cultured vascular smoothmuscle cell)

show abstract

“…The study suggested that cGMP egression appears to be mainly an active transport process which is temperature-dependent. In cultured vascular smooth muscle cells, the decrease in receptor bound 125 I-labeled ANP due to internalization, degradation, and elimination of ligands was more rapid at 37°C than that at 4°C (15). A more recent FIG.…”

Section: Discussionmentioning

confidence: 94%

Membranes for Endotoxin Removal from Dialysate: Considerations on Feasibility of Commercial Ceramic Membranes

Bender¹,

Pflänzel²,

Saunders³

et al. 2000

Artificial Organs

View full text Add to dashboard Cite

As the quality of water in dialysis fluid varies considerably, dialysate is often contaminated by large amounts of bacteria and endotoxins. Membrane properties and operating pressures are acknowledged to give high-flux dialysis with bicarbonate the bacteriological potential to favor passage of endotoxin fragments from the dialysate into the blood stream. Therefore, a sterile dialysate will have to become a standard. Ultrafiltration across hydrophobic synthetic membranes was shown to remove endotoxins (and their fragments) from dialysis water by the combined effect of filtration and adsorption. However, each module can be used for a limited time only. Ceramic membranes may represent an alternative to polymeric membranes for endotoxin removal. In this article, we tested the capacity of different commercial ceramic membranes with nominal molecular weight cut-off down to 1,000 to retain endotoxins from Ps. aeruginosa. The tested membranes did not generally produce dialysate meeting the Association for the Advancement of Medical Instrumentation standard. When using aluminum-containing membranes, we detected aluminum leaking into the dialysate that could possibly be transported into the blood stream.

show abstract

Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

Cited by 8 publications

References 9 publications

Three molecular forms of atrial natriuretic peptides: quantitative analysis and biological characterization

Three molecular forms of atrial natriuretic peptides: quantitative analysis and biological characterization

A dicarba analog of β‐atrial natriuretic peptide (β‐ANP) inhibits guanosine 3′,5′‐cyclic monophosphate production induced by α‐ANP in cultured rat vascular smooth muscle cells

Membranes for Endotoxin Removal from Dialysate: Considerations on Feasibility of Commercial Ceramic Membranes

Contact Info

Product

Resources

About