Heterogeneous regulation of renal atrial natriuretic factor receptor subtypes in one-kidney, one clip hypertensive rats

Bonhomme, Marie-Chantal; García, Raúl

doi:10.1097/00004872-199304000-00009

Cited by 5 publications

(3 citation statements)

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“…One reason for this discrepancy might be the different rat strain used, WKY rats in our study and Sprague-Dawley rats in others (Bonhomme & García 1993). Alternatively, we have found that the amount of kidney hypertrophy in 1K and 1K/1C rats is similar under our conditions, while in other studies, the kidneys in 1K/1C rats showed significantly less hypertrophy than those in 1K rats (García et al 1988).…”

Section: Discussioncontrasting

confidence: 61%

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

Woodard

Li²,

Rosado³

2005

Journal of Molecular Endocrinology

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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 (ANP 1-28 ) binding sites in rat kidney. Here we report an increased B max value of glomerular binding sites for ANP 1-28 and C-type natriuretic peptide 1-22 (CNP ) in hypertrophied and developing kidney, without modifying their affinity, an effect that was prevented in the presence of the synthetic des [Gln 18 , Ser 19 , Gly 20 , Leu 21 , Gly 22 ]ANP 4-23 -amide (C-ANF), suggesting that natriuretic peptide receptor (NPR)-C binding sites might be enhanced. The enhanced B max was only detected in the high affinity binding site for CNP , 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 ANP 1-28 , CNP 1-22 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 B max 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.

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Section: Discussioncontrasting

confidence: 61%

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

Woodard

Li²,

Rosado³

2005

Journal of Molecular Endocrinology

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“…A similar elevation of ANP in plasma of rats with different forms of 'benign' experimental hypertension leads to receptor downregulation (Bonhomme and Garcia, 1993;Garcia et al, 1988;Gauquelin et al, 1988;Schiffrin and St.-Louis, 1987), Down-regulation of ANP receptors has also been found in cortical glomeruli and in glomerular membranes from the spontaneously hypertensive rats of the Okamoto strain (Brown etaL, 1990a, Garcia etal., 1989.…”

Section: Discussionmentioning

confidence: 96%

Atrial-Natriuretic-Peptide Receptors in Glomerular Cryosections of Renal Malignant and Spontaneously Hypertensive Rats

Marin-Grez

Grigelat²,

Heinz‐Erian³

et al. 1995

Biological Chemistry Hoppe-Seyler

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ANP-receptors affinities (KD) and capacities (Bmax) were assayed in cryosections of glomeruli from 'malignant' hypertensive rats (2K-1C) and spontaneously hypertensive rats (PHR). Plasma ANP concentration was twofold higher in 2K-1C (P < 0.05) and PHR (P < 0.02) than in the respective controls, KD and Bmax for rANP99-126 and ANP103-123 did not differ. ANP mediated cGAMP release in 2K-1C rats was also unaffected. ANP-C glomerular receptors (i.e. displacement of tracer binding with ANP103-123) were not down-regulated and had unchanged peptide binding affinity in either kidney of rats with 'malignant' hypertension and in PHR. The difference between Bmax for rANP99-126 and Bmax for rANP103-123 (ANP-A receptor binding) indicates moderate up-regulation of ANP-A receptors in the clipped, and down-regulation in the contralateral kidney of 2K-1C (2K-1C, right vs. left, P < 0.05). Since [ANP]pl, and also Bmax and KD for ANP were similar in both hypertension models investigated, changes of the [ANP]pl/ANP-receptor system can not completely explain the marked natriuresis of rats with 'malignant' hypertension.

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“…The sequence analysis of the promoter region has identified putative cis -acting binding sites for the known transcription factors, but the functional significance of most of these sites remains to be elucidated. Although transcriptional regulation of the Npr1 gene is poorly understood, the activity and expression of NPRA is regulated by various factors, including natriuretic peptides [67-74], hormones such as endothelin [75], glucocorticoids [76-79], angiotensin II [80-85], growth factors [67, 86, 87], extracellular ion composition [88-93], pregnancy [94-98], physiological and pathophysiological conditions [99-108], and transcription factors [109-111]. A better understanding of the regulation of NPRA expression depends on more extensive functional characterization of its promoter region and elucidation of the functional significance of the potential cis -elements in this region, which are responsible for the binding of known transacting factors.…”

Section: Introductionmentioning

confidence: 99%

Ligand-mediated endocytosis and intracellular sequestration of guanylyl cyclase/natriuretic peptide receptors: role of GDAY motif

Pandey

2009

Mol Cell Biochem

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The guanylyl cyclase/natriuretic peptide receptor-A (GC-A/NPRA), also referred to as GC-A, is a single polypeptide molecule having a critical function in blood pressure regulation and cardiovascular homeostasis. GC-A/NPRA, which resides in the plasma membrane, consists of an extracellular ligand-binding domain, a single transmembrane domain, and an intracellular cytoplasmic region containing a protein kinase-like homology domain (KHD) and a guanylyl cyclase (GC) catalytic domain. After binding with atrial and brain natriuretic peptides (ANP and BNP), GC-A/NPRA is internalized and sequestered into intracellular compartments. Therefore, GC-A/NPRA is a dynamic cellular macromolecule that traverses different subcellular compartments through its lifetime. This review describes the roles of short-signal sequences in the internalization, trafficking, and intracellular redistribution of GC-A/NPRA from cell surface to cell interior. Evidence indicates that, after internalization, the ligand-receptor complexes dissociate inside the cell and a population of GC-A/NPRA recycles back to the plasma membrane. Subsequently, the disassociated ligands are degraded in the lysosomes. However a small percentage of the ligand escapes the lysosomal degradative pathway and is released intact into culture medium. By using pharmacologic and molecular perturbants, emphasis has been placed on the cellular regulation and processing of ligand-bound GC-A/NPRA in terms of receptor trafficking and down-regulation in intact cells. The discussion is concluded by examining the functions of short-signal sequence motifs in the cellular life-cycle of GC-A/NPRA, including endocytosis, trafficking, metabolic processing, inactivation, and/or down-regulation in model cell systems.

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Heterogeneous regulation of renal atrial natriuretic factor receptor subtypes in one-kidney, one clip hypertensive rats

Cited by 5 publications

References 0 publications

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

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

Atrial-Natriuretic-Peptide Receptors in Glomerular Cryosections of Renal Malignant and Spontaneously Hypertensive Rats

Ligand-mediated endocytosis and intracellular sequestration of guanylyl cyclase/natriuretic peptide receptors: role of GDAY motif

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