Evidence for Atrial Natriuretic Factor Induced Natriuretic Peptide Receptor Subtype Switching in Rat Proximal Tubular Cells during Culture

1998 ◽  
Vol 6 (2) ◽  
pp. 104-111 ◽  
Author(s):  
Sanjay K. Mistry ◽  
Prabal K. Chatterjee ◽  
Roshan P. Weerackody ◽  
Gabrielle M. Hawksworth ◽  
Rachel M. Knott ◽  
...  
Keyword(s):  
Natriuretic Peptide ◽  
Atrial Natriuretic Factor ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Peptide Receptor ◽  
Natriuretic Factor ◽  
Proximal Tubular ◽  
Atrial Natriuretic

The expression and secretion of atrial natriuretic factor and brain natriuretic peptide by rat proximal tubular cells

2000 ◽  
Vol 59 (7) ◽  
pp. 783-790 ◽  
Author(s):  
Sanjay Mistry ◽  
Benedict Lussert ◽  
Keith Stewart ◽  
Gabrielle M Hawksworth ◽  
Alan Struthers ◽  
...  
Keyword(s):  
Brain Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Atrial Natriuretic Factor ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Natriuretic Factor ◽  
Proximal Tubular ◽  
Atrial Natriuretic

Atrial Natriuretic Factor and Angiotensin Ii Stimulate Nitric Oxide Release from Human Proximal Tubular Cells

1995 ◽  
Vol 89 (5) ◽  
pp. 527-531 ◽  
Author(s):  
J. S. McLay ◽  
P. K. Chatterjee ◽  
S. K. Mistry ◽  
R. P. Weerakody ◽  
A. G. Jardine ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Angiotensin Ii ◽  
Atrial Natriuretic Factor ◽  
Nitric Oxide Production ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Oxide Production ◽  
Natriuretic Factor ◽  
Proximal Tubular ◽  
Atrial Natriuretic

1. It has been recently reported that angiotensin II can enhance atrial natriuretic factor-stimulated cyclic GMP release from brain capillary endothelial cells and stimulate directly the release of cyclic GMP by Neuro 2a cells. A possible mechanism mediating such cyclic GMP release could be via the production of nitric oxide and the resultant stimulation of soluble guanylate cyclase. 2. The ability of angiotensin II, atrial natriuretic factor and c(4–23) atrial natriuretic factor to stimulate nitric oxide production was investigated in primary cultures of human proximal tubular cells. 3. Freshly prepared human proximal tubular cells were seeded onto 6-well plates and allowed to reach confluence. Cells were then incubated with incremental concentrations of either angiotensin II, atrial natriuretic factor or c(4–23) atrial natriuretic factor alone for 1, 4, 12 or 24 h or in the presence of the nitric oxide synthase inhibitor NG-monomethyl-l-arginine. Angiotensin II was also incubated with human proximal tubular cells in the presence of the AT, and AT2 receptor antagonists DuP 753 and PD 123319. 4. Incubation of human proximal tubular cells with angiotensin II, atrial natriuretic factor or c(4–23) atrial natriuretic factor produced a dose- and time-dependent increase in nitric oxide production, which was inhibited in the presence of NG-monomethyl-l-arginine. A similar increase in nitric oxide production was observed after incubation with atrial natriuretic factor or c(4–23) atrial natriuretic factor. 5. The angiotensin-induced increase in nitric oxide production was not inhibited in the presence of either the angiotensin AT1 or AT2 receptor antagonists DuP 753 or PD 123319. 6. This study demonstrates that primary cultures of human proximal tubular cells can be stimulated to produce nitric oxide by both atrial natriuretic factor and angiotensin II. Furthermore, the atrial natriuretic factor-induced response appears to be mediated via the atrial natriuretic factor-C receptor, while the angiotensin II-induced response appears to be mediated by a novel, as yet unidentified, angiotensin II receptor.

Atrial Natriuretic Factor and Angiotensin II Stimulate the Production of Nitric OXIDE in Human Proximal Tubular Cells: A new Autoregulatory Mechanism

1995 ◽  
Vol 89 (s33) ◽  
pp. 23P-23P
Author(s):  
PK Chatteijee ◽  
S Mistry ◽  
S McKay ◽  
R Weerackody ◽  
GM Hawksworth ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Angiotensin Ii ◽  
Atrial Natriuretic Factor ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Natriuretic Factor ◽  
Proximal Tubular ◽  
Autoregulatory Mechanism ◽  
Atrial Natriuretic

Atrial natriuretic factor binding sites in rat area postrema: autoradiographic study

1992 ◽  
Vol 263 (4) ◽  
pp. R747-R755 ◽  
Author(s):  
E. M. Konrad ◽  
G. Thibault ◽  
E. L. Schiffrin
Keyword(s):  
Natriuretic Peptide ◽  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Cellular Localization ◽  
Area Postrema ◽  
Receptor Subtype ◽  
Electron Microscopic ◽  
Electron Microscopic Autoradiography ◽  
Natriuretic Factor ◽  
Atrial Natriuretic

The area postrema (AP) is a brain stem circumventricular organ implicated, among other functions, in central cardiovascular (CV) regulation. Competition binding analysis performed by quantitative in vitro autoradiography demonstrated specific, high-affinity (Kd, 0.32 +/- 0.11 nM), low-capacity (Bmax, 57.5 +/- 10.9 fmol/mg protein) atrial natriuretic factor (ANF) binding sites in the AP. C-ANF [des-(Gln116-Gly120)ANF-(Arg102-Cys121)-NH2] and ANF-(Phe106-Ile113)-NH2 (two ligands endowed with selectivity for the ANF-C receptor), as well as C-type natriuretic peptide (CNP), did not compete noticeably at pathophysiological concentrations for 125I-ANF binding. 125I-[Tyr0]CNP bound to the AP to a much lower extent than 125I-ANF. Electron microscopic autoradiography in vivo disclosed that 125I-ANF was preferentially bound to axon, dendrite, and astrocyte plasmalemma. These studies demonstrate that the AP contains natriuretic peptide binding sites with pharmacological characteristics of the ANF-A and ANF-B but not of the ANF-C receptor subtype. In the AP, ANF interacts with those sites resembling ANF-A receptors. Cellular localization of these binding sites may relate to their possible involvement in the centrally mediated salt and water regulation and/or CV effects of circulating ANF.

Expression and function of natriuretic peptide receptor subtype A (NPR-A) in antrum and fundus of rat and human stomach

2001 ◽  
Vol 120 (5) ◽  
pp. A311-A311
Author(s):  
W GOWERJR ◽  
S PREMARATNE ◽  
R MCCUEN ◽  
M SCHUBERT
Keyword(s):  
Natriuretic Peptide ◽  
Human Stomach ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
And Function ◽  
Subtype A

Allotopic antagonism of the non-peptide atrial natriuretic peptide (ANP) antagonist HS-142-1 on natriuretic peptide receptor NPR-A

2002 ◽  
Vol 362 (2) ◽  
pp. 231-237 ◽  
Author(s):  
Hugo POIRIER ◽  
Jean LABRECQUE ◽  
Julie DESCHÊNES ◽  
André DeLÉAN
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Mode Of Action ◽  
Transmembrane Domain ◽  
Peptide Binding ◽  
Natriuretic Peptide Receptor ◽  
Receptor Dimerization ◽  
Peptide Receptor ◽  
Peptide Binding Site ◽  
Atrial Natriuretic

The microbial polysaccharide HS-142-1 has been documented as an antagonist of natriuretic peptides. It inhibits activation and peptide binding to both guanylate receptors natriuretic peptide receptor (NPR)-A and NPR-B, but has no effect on the non-cyclase receptor NPR-C. At first sight the effect of HS-142-1 on peptide binding appears to be surmountable, suggesting that it might be competitive despite its chemically divergent nature. We explored its mode of action on wild-type NPR-A (WT), on a disulphide-bridged constitutively active mutant (C423S) and on truncated mutants lacking either their cytoplasmic domain (ΔKC) or both the cytoplasmic and the transmembrane domains (ECD). On the WT, HS-142-1 inhibited atrial natriuretic peptide (ANP) binding with a pK value of 6.51±0.07 (Kd = 0.31μM). It displayed a similar effect on the C423S mutant (pK = 6.31±0.11), indicating that its action might not be due to interference with receptor dimerization. HS-142-1 also inhibited ANP binding to ΔKC with a pK of 7.05±0.05 (Kd = 0.089μM), but it was inactive on ANP binding to ECD at a concentration of 10−4M, suggesting that the antagonism was not competitive at the peptide-binding site located on the ECD and that the transmembrane domain might be required. HS-142-1 also enhanced dissociation of NPR-A-bound 125I-ANP in the presence of excess unlabelled ANP, implying an allotopic (allosteric) mode of action for the antagonist.

scholarly journals Structure of the bovine atrial natriuretic peptide receptor (type C) gene

1991 ◽  
Vol 266 (17) ◽  
pp. 11122-11125
Author(s):  
T. Saheki ◽  
T. Mizuno ◽  
T. Iwata ◽  
Y. Saito ◽  
T. Nagasawa ◽  
...  
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Receptor Type ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
Type C ◽  
Atrial Natriuretic Peptide Receptor ◽  
Atrial Natriuretic
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