scholarly journals Regulation of Natriuretic Peptide Receptors by Thyrotropin in FRTL-5 Rat Thyroid Cells: Evidence for Nonguanylate Cyclase Atrial Natriuretic Factor-Binding Sites in Cells Lacking the Natriuretic Peptide Receptor C

Endocrinology ◽  
1999 ◽  
Vol 140 (3) ◽  
pp. 1365-1374 ◽  
Author(s):  
Donald F. Sellitti ◽  
Sonia Q. Doi
Keyword(s):  
Natriuretic Peptide ◽  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Natriuretic Peptide Receptor ◽  
Thyroid Cells ◽  
Natriuretic Peptide Receptors ◽  
Peptide Receptor ◽  
Factor Binding ◽  
Natriuretic Factor ◽  
Rat Thyroid

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

scholarly journals cAMP inhibits natriuretic peptide receptor-B activity and increases C-type natriuretic peptide in FRTL-5 rat thyroid cells

2004 ◽  
Vol 180 (1) ◽  
pp. 23-34 ◽  
Author(s):  
DF Sellitti ◽  
E Puggina ◽  
C Lagranha ◽  
SQ Doi
Keyword(s):  
Protein Kinase ◽  
Real Time ◽  
Natriuretic Peptide ◽  
Real Time Pcr ◽  
Camp Signaling ◽  
Ionophore A23187 ◽  
Natriuretic Peptide Receptor ◽  
Thyroid Cells ◽  
Peptide Receptor ◽  
Rat Thyroid

C-type natriuretic peptide (CNP) and its cognate guanylyl cyclase receptor, the natriuretic peptide receptor B (NPR-B) together constitute a regulatory system that controls cell function via the generation of intracellular cyclic GMP. In this report we have examined the role of cAMP signaling in the regulation of CNP and NPR-B activity in the FRTL-5 rat thyroid follicular cell line. As had been observed earlier with TSH, the cAMP mimetic, dibutyryl cAMP (dbcAMP; 1 mM) induced a significant reduction in CNP-stimulated cGMP generation that was first apparent after 6 h of treatment. The inhibitory effect of dbcAMP on NPR-B was dose dependent, with an EC50 of 0.2 mM. Pretreatment of FRTL-5 cells with either of two protein kinase A (PKA) inhibitors, KT-5720 and H-89, failed to curtail the dbcAMP reduction in NPR-B activity, suggesting that the cAMP pathway leading to inhibition of NPR-B is PKA independent. Whereas either a 30-min or a 24-h treatment with the protein kinase C-activator phorbol myristate acetate failed to alter maximal levels of CNP-stimulated cGMP, a 24-h exposure to the calcium ionophore A23187 reduced CNP-stimulated cGMP to about one-third of control. Pretreatment of FRTL-5 cells with the cell-permeable calcium chelator 1,2 bis(2-aminophenoxy)ethane-N,N,N1,N1-tetraacetic acid, tetraacetoxymethyl ester completely abrogated the cAMP-induced reduction of CNP-stimulated cGMP. Real-time PCR showed no effect of dbcAMP on NPR-B transcript at 3 and 6 h, but indicated a 40% reduction in transcript by dbcAMP at 24 h. In contrast, real-time PCR indicated a 5-fold increase in CNP transcript at 3 h, reaching 15.4-fold above control at 6 h in cells treated with dbcAMP. In addition, immunofluorescence staining of FRTL-5 cells with a specific antibody for CNP-22 showed the presence of cytoplasmic CNP that was up-regulated by incubation with either TSH or dbcAMP. These results suggested that cAMP signaling regulates the natriuretic peptide system in rat thyroid cells by increasing CNP expression, and reducing NPR-B activity. This latter action of cAMP appears to be both PKA independent and calcium dependent, and provides support for a dominant role for calcium in the regulation of NPR-B in the rat thyroid.

scholarly journals Characteristics of the renal C-type natriuretic peptide receptor in hypertrophied and developing rat kidney

2005 ◽  
Vol 35 (3) ◽  
pp. 519-530 ◽  
Author(s):  
G E Woodard ◽  
Xiaohong Li ◽  
J A Rosado
Keyword(s):  
Natriuretic Peptide ◽  
Binding Sites ◽  
Rat Kidney ◽  
Protein A ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
Camp Synthesis ◽  
Inhibitory Role ◽  
Developing Kidney ◽  
Old Rats

This study investigates the effect of hypertrophy, using one kidney and one kidney/one clip rats, and development, comparing 3- and 12-week-old rats, on the expression of the 28-amino acid atrial natriuretic peptide (ANP1–28) binding sites in rat kidney. Here we report an increased Bmax value of glomerular binding sites for ANP1–28 and C-type natriuretic peptide 1–22 (CNP1–22) in hypertrophied and developing kidney, without modifying their affinity, an effect that was prevented in the presence of the synthetic des[Gln18, Ser19, Gly20, Leu21, Gly22]ANP4–23-amide (C-ANF), suggesting that natriuretic peptide receptor (NPR)-C binding sites might be enhanced. The enhanced Bmax was only detected in the high affinity binding site for CNP1–22, which has been identified as the 67 kDa NPR-C-like protein. A similar effect was observed in renal glomeruli from 3-week-old rats compared with 12-week-old rats. Our results indicate that ANP1–28, CNP1–22 and C-ANF inhibited cAMP synthesis stimulated by the physiological agonists histamine and 5-hydroxytryptamine or directly by forskolin. The inhibitory effect was found to be significantly greater in 1-kidney and 1-kidney/1-clip rats than in controls, and in 3-week-old rats compared with 12-week-old rats. Our observations suggest that this effect must be attributed to the 67 kDa NPR-C-like protein due to the enhanced Bmax values and the reported inhibitory role for this receptor on adenylyl cyclase activity. The enhanced inhibitory role of natriuretic peptides on cAMP synthesis in hypertrophied and developing kidney may influence glomerular function in the rat kidney and suggests a role for the 67 kDa NPR-C-like protein in growth.

Radioautographic Localization of 125I-Atrial Natriuretic Factor Binding Sites in the Brain

1986 ◽  
Vol 44 (3) ◽  
pp. 365-372 ◽  
Author(s):  
Césario Bianchi ◽  
J. Gutkowska ◽  
M. Ballak ◽  
G. Thibault ◽  
R. Garcia ◽  
...  
Keyword(s):  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Factor Binding ◽  
Natriuretic Factor ◽  
The Brain ◽  
Atrial Natriuretic

Thyrotropin Modulates Receptor-Mediated Processing of the Atrial Natriuretic Peptide Receptor in Cultured Thyroid Cells*

1991 ◽  
Vol 72 (3) ◽  
pp. 669-674 ◽  
Author(s):  
YUEH-CHU L. TSENG ◽  
KENNETH D. BURMAN ◽  
SABITA LAHIRI ◽  
MAGED M. ABDELRAHIM ◽  
JUAN C. D’AVIS ◽  
...  
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Natriuretic Peptide Receptor ◽  
Thyroid Cells ◽  
Peptide Receptor ◽  
Atrial Natriuretic Peptide Receptor ◽  
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.

Cloning and functional expression of the bovine natriuretic peptide receptor-B (natriuretic factor R1c subtype)

1994 ◽  
Vol 137 (2) ◽  
pp. 173-182 ◽  
Author(s):  
Randy Fenrick ◽  
Kasimir Babinski ◽  
Normand McNicoll ◽  
Marc Therrien ◽  
Jacques Drouin ◽  
...  
Keyword(s):  
Natriuretic Peptide ◽  
Functional Expression ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
Natriuretic Factor
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