Effect of native and synthetic atrial natriuretic factor on cyclic GMP

Hamet, Pavel; Tremblay, Johanne; Pang, Stephen C.; García, Raúl; Thibault, Gaétan; Gutkowska, Jolanta; Cantin, M.; Genest, Jacques

doi:10.1016/0006-291x(84)90260-2

Cited by 348 publications

(99 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It should be also of note that SHR had higher initial blood pressure levels and responded greater than WKY to the hypotensive effect of infused ANP, suggesting that natriuresis induced by ANP in both strains could be modified by several factors other than cGMP-related changes. In the present study, we confirmed the previous findings showing positive relationship between urinary cGMP excretion and urine flow or urinary sodium excretion in anesthetized rats during AP infusion (Hamet et al 1984;Gerzer et al 1985). These results are in good accordance with the recent observations that vasodilatory action of ANP correlated well with venous plasma cGMP concentration during the continuous infusion of ANP in human (Fujita et al 1987).…”

Section: Discussionsupporting

confidence: 93%

“…Such a close relationship between ANP and cGMP has also been found in vivo. When atrial extracts or synthetic ANP were infused into rats or in man, plasma cGMP levels and urinary excretion of cGMP markedly rose (Hamet et al 1984 ;Gerzer et al 1985). Furthermore, concomitant increase in plasma ANP and cGMP has been observed in normal volunteers during saline infusion (Weil et al 1985).…”

Section: Discussionmentioning

confidence: 99%

“…ANP increases cGMP levels in various tissues including vasculature, adrenal gland and kidney, and in cultures of vascular endothelial or smooth muscle cells, renal tubules and glomerular mesangium (Hamet et al 1984 Sato et al 1986b ; Stokes et al 1986). It is well known that ANP selectively dilates renal artery (Oshima et al 1984), and we have previously reported that the stimulatory effect of atriopeptin (AP) III on intracellular cGMP levels was greater in cultured vascular smooth muscle (VSM) cells from renal artery than those from mesenteric artery (Sato et al 1986b).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Cyclic GMP accumulation by atriopeptins in cultured rat renal and vascular smooth muscle cells.

Sato¹,

Abe

Takeuchi³

et al. 1988

Tohoku J. Exp. Med.

View full text Add to dashboard Cite

To evaluate the role of cyclic guanosine monophosphate (cGMP) in the vascular and renal action of atrial natriuretic peptide (ANP), we compared the effects of atriopeptins (APs) on cGMP accumulation in cultured cells from rat mesenteric vascular smooth muscle (VSM), glomerular mesangium (GM) and renal papillary collecting tubule (RPCT), and also evaluated the relationship between renal sodium or water excretion and urinary cGMP in AP-infused rats. Both AP I and AP III increased intracellular cGMP levels dose-dependently in all types of cells, while they did not affect intracellular cAMP levels or prostaglandin synthesis.AP III was 100 times more potent than AP I. The magnitude change in cGMP levels was largest in GM cells. The sensitivity of VSM and GM cells to AP III were greater than that of RPCT cells. There were significant positive relationships between urinary excretion of sodium or water and that of cGMP levels in AP-infused rats. These results may suggest that GM and VSM cells are the principal targets for ANP to stimulate cGMP synthesis and, possibly, to exert the renal sodium and water excretion, and also support the hypothesis that cGMP mediates the cellular action of ANP. atrial natriuretic peptide ; cyclic GMP ; glomerular mesangium ; papillary collecting tubule ; vascular smooth muscle Atrial natriuretic peptide (ANP) is a hormone which has a potent natriuretic, diuretic and direct vasorelaxant action (DeBold et al. 1981;Maack et al. 1985;. ANP is the only biological substance which has

show abstract

Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Cyclic GMP accumulation by atriopeptins in cultured rat renal and vascular smooth muscle cells.

Sato¹,

Abe

Takeuchi³

et al. 1988

Tohoku J. Exp. Med.

View full text Add to dashboard Cite

show abstract

“…These actions of ANP are brought about via the activation of membrane-bound protein, natriuretic peptide receptor type A (NPR-A), or guanylyl cyclase A. [2][3][4] NPR-A is a 130-KDa transmembrane protein containing an ANP-binding motif at its extracellular NH 2 terminus and GC activity at its COOH-terminal intracellular domain. 5 Activation of NPR-A leads to the conversion of GTP to the intracellular second messenger cGMP, which is involved in most of the biological responses associated with natriuretic peptides.…”

mentioning

confidence: 99%

“…5 Activation of NPR-A leads to the conversion of GTP to the intracellular second messenger cGMP, which is involved in most of the biological responses associated with natriuretic peptides. [2][3][4][5] Increased cGMP yields receptor desensitization, resulting in a decrease of ANP-stimulated cGMP synthesis. 6 Receptor preoccupancy appears to be a mechanism of apparent receptor desensitization 7 but transfection experiments with NPR-A cDNA have revealed that early desensitization by ANP pretreatment can be due to dephosphorylation of NPR-A protein.…”

mentioning

confidence: 99%

Characterization of a cGMP-Response Element in the Guanylyl Cyclase/Natriuretic Peptide Receptor A Gene Promoter

et al. 2004

Self Cite

View full text Add to dashboard Cite

Abstract-Previous studies have shown that atrial natriuretic peptide (ANP) can inhibit transcription of its receptor, guanylyl cyclase A, by a mechanism dependent on cGMP and have suggested the presence of a putative cGMP-response element (cGMP-RE) in the Npr1 gene promoter. To localize and characterize the putative cis-acting element, we have subcloned a 1520-bp fragment of the rat Npr1 promoter in an expression vector containing the luciferase reporter gene. Several fragments, generated by exonuclease III-directed deletions, were transiently transfected into cells to measure their promoter activity. Deletion from Ϫ1520 to Ϫ1396 of a 1520-bp-long Npr1 promoter led to a 5-fold increase in luciferase activity. Subsequent deletion to the position Ϫ1307 resulted in a decrease of luciferase activity by 90%. Preincubation of cells with 100 nM of ANP or 100 M 8-bromo-cGMP inhibited luciferase activity of the 1520-bp and 1396-bp-long fragments, but not the activity of the 1307-bp fragment, suggesting that the cGMP-RE is localized between positions Ϫ1396 and Ϫ1307. The cGMP regulatory region was narrowed by gel shift assays and footprinting to position Ϫ1372 to Ϫ1354 from the transcription start site of Npr1 and indicated its interaction with transcriptional factor(s). Cross-competition experiments with mutated oligonucleotides led to the definition of a consensus sequence (Ϫ1372 AaAtRKaNTTCaAcAKTY Ϫ1354) for the novel cGMP-RE, which is conserved in the human (75% identity) and mouse (95% identity) Npr1 promoters. Key Words: cyclic GMP Ⅲ natriuretic peptides Ⅲ receptors, atrial natriuretic factor A trial natriuretic peptide (ANP) is a cardiac hormone with potent effects in the kidney, vasculature, and nervous system. It has vasorelaxant activity in vascular smooth muscle and promotes urinary sodium and water excretion by the kidney (for review, see Reference 1 ). These actions of ANP are brought about via the activation of membrane-bound protein, natriuretic peptide receptor type A (NPR-A), or guanylyl cyclase A. 2-4 NPR-A is a 130-KDa transmembrane protein containing an ANP-binding motif at its extracellular NH 2 terminus and GC activity at its COOH-terminal intracellular domain. 5 Activation of NPR-A leads to the conversion of GTP to the intracellular second messenger cGMP, which is involved in most of the biological responses associated with natriuretic peptides. 2-5 Increased cGMP yields receptor desensitization, resulting in a decrease of ANP-stimulated cGMP synthesis. 6 Receptor preoccupancy appears to be a mechanism of apparent receptor desensitization 7 but transfection experiments with NPR-A cDNA have revealed that early desensitization by ANP pretreatment can be due to dephosphorylation of NPR-A protein. 8 Besides, a previous study demonstrated that NPR-A activity, as well as its mRNA levels, is diminished in a time-and concentration-dependent manner by ANP or by a cell-permeable cGMP analog, 8-bromo-cGMP. 9 Those results suggest transcriptional regulation via a putative cGMPresponse element (cGMP-RE) in the p...

show abstract