Specific binding of atrial natriuretic peptide to rat mesenteric artery: Effect of calcium and 5-guanylylimidodiphosphate

1987 ◽  
Vol 73 (6) ◽  
pp. 573-579 ◽  
Author(s):  
Fiona Lyall ◽  
J. J. Morton
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Binding Sites ◽  
Mesenteric Artery ◽  
Guanosine Triphosphate ◽  
High Affinity ◽  
Dissociation Equilibrium ◽  
Rat Mesenteric Artery ◽  
Receptor Number ◽  
Atrial Natriuretic

1. High-dissociation equilibrium constant (20 pmol/l, receptor number 17 fmol/mg) and low-dissociation equilibrium constant (10 nmol/l, receptor number 5 nmol/mg) affinity binding sites for atrial natriuretic peptide have been identified in membrane preparations from rat mesenteric artery. 2. Tracer degradation was corrected for mathematically and binding data were analysed by a non-linear computer technique. 3. Non-atrial natriuretic peptide vasoactive hormones, angiotensin II, vasopressin and bradykinin, did not compete for the high-affinity site. Related peptides with either C- or N-terminal amino acids missing still competed, while peptides without an intact disulphide bridge did not compete. 4. Neither the addition nor the removal of calcium affected the affinity or density of binding sites. Also the non-hydrolysable guanosine triphosphate analogue 5-guanylylimidodiphosphate had no effect on either affinity or number of sites. 5. These results indicate the presence of a specific high-affinity vascular receptor for atrial natriuretic peptide which could interact with the hormone under physiological conditions. The mechanism of binding is uncertain but is unlikely to involve calcium- or guanosine triphosphate-associated regulatory sites.

Atrial natriuretic peptide vascular receptor: regulation of low-affinity binding by calcium

1989 ◽  
Vol 76 (1) ◽  
pp. 9-11 ◽  
Author(s):  
J. J. Morton ◽  
Elisabeth C. Beattie ◽  
Fiona Lyall
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Plasma Membranes ◽  
Affinity Binding ◽  
High Affinity ◽  
Dissociation Equilibrium ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Vascular Receptor ◽  
Atrial Natriuretic

1. In the presence of calcium, both high- [dissociation equilibrium constant (Kd) 5.8 × 10−11 mol/l] and low-(Kd 1.2 × 10−8 mol/l) affinity binding of atrial natriuretic peptide was detected on plasma membranes prepared from sodium-depleted rats. 2. In contrast, under calcium-free conditions only high-affinity binding (Kd 6.9 × 10−11 mol/l) was detected. 3. The requirement for calcium for low-affinity binding suggests a different mechanism of action than that for the high-affinity receptor.

Vascular angiotensin II and atrial natriuretic peptide receptors in normal and growth-retarded human placentae

1990 ◽  
Vol 126 (2) ◽  
pp. 341-347 ◽  
Author(s):  
J. McQueen ◽  
J. C. P. Kingdom ◽  
A. G. Jardine ◽  
J. M. C. Connell ◽  
M. J. Whittle
Keyword(s):  
Angiotensin Ii ◽  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Dissociation Equilibrium ◽  
Vascular Responsiveness ◽  
High Affinity Receptor ◽  
Receptor Number ◽  
Affinity Receptor ◽  
Human Placentae ◽  
Atrial Natriuretic

ABSTRACT Receptors for angiotensin II (AII) and atrial natriuretic peptide (ANP) were characterized in a membrane fraction from resistance-type artery from human placentae. Placentae from normal pregnancies and pregnancies complicated by intrauterine growth retardation (IUGR) were studied. High- and low-affinity receptors for AII (dissociation equilibrium constant (Kd) 1 ·7 and 15·7 nmol/l respectively) and ANP (Kd 0·2 and 55·5 nmol/l respectively) were identified; these parameters were unchanged in IUGR, but there was a reduction in high-affinity receptor number by approximately 50% for AII and 80% for ANP in this condition. Both peptides may have a role in the regulation of fetoplacental blood flow. The alterations in IUGR are consistent with sustained activation of the fetal reninangiotensin system and suggest altered vascular responsiveness to ANP. Journal of Endocrinology (1990) 126, 341–347

Specific endothelin binding sites in renal medullary collecting duct cells: lack of interaction with ANP binding and cGMP signalling

1992 ◽  
Vol 70 (8) ◽  
pp. 1167-1174 ◽  
Author(s):  
Peter Cernacek ◽  
Louis Legault ◽  
Duncan J. Stewart ◽  
Mortimer Levy
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Binding Sites ◽  
Collecting Duct ◽  
Specific Cell ◽  
Binding Studies ◽  
Single Class ◽  
High Affinity ◽  
Medullary Collecting Duct ◽  
Atrial Natriuretic

The diverse biological actions of endothelins (ET) appear to be mediated by specific cell-surface receptors. Autoradiography and membrane binding studies have shown abundant ET binding sites in the kidney. However, their expression in specific types of renal cells is unclear. We studied the binding of 125I-labelled endothelin-1 in freshly isolated cell suspensions from canine inner medullary collecting duct. Competition binding experiments revealed the presence of specific high-affinity binding sites: unlabelled ET-1 and ET-2 competed with the radioligand with an IC50 of 135 and 83 pM, respectively, while the IC50 of ET-3 and big ET-1 were 2 and 4 orders of magnitude higher, indicating the presence of ETA-type receptor. Angiotensin II, vasopressin, and atrial natriuretic peptide (ANP) did not compete for ET binding even at a concentration of 10−6 M. Saturation binding experiments showed a single class of binding sites of high density (Bmax = 56.7 ± 10.3 fmol/106 cells) and high affinity (Kd = 69.8 ± 10 pM). In contrast, ANP receptors in the same cell preparations appeared as two classes of binding sites with widely different affinity and density. The high-affinity ANP site (Kd = 311 ± 48 pM) was compatible with ANP-B (guanylate cyclase-coupled) receptor. ET-1 did not compete for this receptor. ET-1 (10−7 M) did not alter ANP-induced cGMP generation in these cells (3.8-fold increase at 10−7 M ANP), nor basal levels of cGMP. The expression by the distal tubular epithelium of specific ET-1 binding sites strongly suggests the presence of a functional receptor, which may mediate the inhibition of Na+ transport in these cells. The mechanism and the transduction pathway of this effect appear to be different and independent from those of ANP.Key words: endothelin receptor, distal collecting duct, atrial natriuretic peptide receptor, cGMP generation.

scholarly journals α-rat atrial natriuretic peptide(rANP) receptor binding sites in rat brain microvessels

1988 ◽  
Vol 46 ◽  
pp. 106
Author(s):  
Masa-aki Ibaragi ◽  
Masami Niwa ◽  
Yasufumi Kataoka ◽  
Keisuke Tsutsumi ◽  
Masaki Kurihara ◽  
...  
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Rat Brain ◽  
Natriuretic Peptide ◽  
Receptor Binding ◽  
Binding Sites ◽  
Brain Microvessels ◽  
Atrial Natriuretic

Atrial natriuretic peptide in the eel, Anguilla anguilla L.: its cardiac distribution, receptors and actions on isolated branchial cells

1992 ◽  
Vol 9 (2) ◽  
pp. 103-114 ◽  
Author(s):  
C. L. Broadhead ◽  
U. T. O'Sullivan ◽  
C. F. Deacon ◽  
I. W. Henderson
Keyword(s):  
Sodium Chloride ◽  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Binding Sites ◽  
Specific Binding ◽  
Anguilla Anguilla ◽  
Chloride Cells ◽  
Dependent Manner ◽  
Single Class ◽  
Atrial Natriuretic

ABSTRACT The presence of atrial natriuretic peptide (ANP) and the nature of its binding sites were studied in freshwater (FW)- and seawater (SW)-adapted eels using a heterologous analogue, that of the rat (rANP). Rat ANP-like immunoreactivity was demonstrated in the cardiac atria and ventricles of both FW and SW eels, and electron-dense ANP-like granules were observed. The atria and ventricles of FW eels contained significantly more granules than those of SW animals and, in both types, the atria were more granular than the ventricles. Specific binding sites for rANP were demonstrated by displacement and uptake experiments using labelled rANP in dispersed eel branchial cell preparations, enriched in chloride cells. The concentration of rANP required to produce a 50% inhibition of binding in FW cells was significantly lower than that in SW cells. Scatchard analyses revealed the presence of two classes of binding site in SW eel branchial cells but only a single class of receptor in FW cells. The affinity of the FW receptor was not significantly different from that of the SW high affinity site. Rat ANP stimulated the production of cyclic GMP (cGMP) in a dose-dependent manner, and both basal and stimulated levels of cGMP were significantly greater in SW branchial cells. These studies suggest that ANP is involved in the adaptation of the euryhaline eel to differing environmental salinities; the levels of the peptide in the heart alter with changing salinity, and the nature of the receptors in the sodium chloride-transporting epithelium of the gill changes in response to the need either to eliminate or to absorb sodium chloride.

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