Transcriptional regulation of guanylyl cyclase/natriuretic peptide receptor-A gene

Kumar, Prerna; Arise, Kiran K; Pandey, Kailash N.

doi:10.1016/j.peptides.2006.01.004

Cited by 11 publications

(22 citation statements)

References 38 publications

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“…Cloning of the Npr1 proximal promoter-luciferase reporter constructs (Ϫ356/ϩ55 bp, Ϫ356/ϩ29 bp, and Ϫ356/-46 bp) have been described (34,35). Cloning of the construct Ϫ356/Ϫ90 bp was done using Ϫ356 forward (5Ј-tacggaacgcgtgagggggggcagcttcctcac-3Ј) and Ϫ90 reverse (5Ј-acgggaccacaaggcgagccaggcagc-3Ј) primers.…”

Section: Methodsmentioning

confidence: 99%

“…The cells were transfected by Lipofectamine 2000 reagent (Invitrogen) between 4 and 16 passages and luciferase activity was measured as described previously (34). The results were normalized for transfection efficiency as relative to light units per Renilla luciferase activity.…”

Section: Methodsmentioning

confidence: 99%

“…Whole Cell Lysate and Nuclear Extract Preparation and Immunoblot Assay-Whole cell lysate and nuclear extract were prepared as described earlier (34). The protein concentration of the lysate was measured with a Bradford protein detection kit (Bio-Rad).…”

Section: Methodsmentioning

confidence: 99%

“…The protein concentration of the lysate was measured with a Bradford protein detection kit (Bio-Rad). Immunoblot assay was done as previously described (34). The cell lysate (60 g of protein) was electrophoresed for 2 h, then transferred to a nylon membrane.…”

Section: Methodsmentioning

confidence: 99%

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Histone Deacetylase Inhibitors Modulate the Transcriptional Regulation of Guanylyl Cyclase/Natriuretic Peptide Receptor-A Gene

Kumar

Tripathi

Pandey

2014

Journal of Biological Chemistry

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Background: Natriuretic peptide receptor-A (NPRA) lowers blood pressure and blood volume. Results: Data show that histone deacetylase inhibitors (HDACi) enhance NPRA expression by blocking HDACs and interacting with Sp1, histone acetyltransferase, and acetylated histones. Conclusion: Results suggest that epigenetic mechanisms regulate NPRA gene transcription. Significance: Findings will help to identify molecular targets regulating NPRA expression and function in vivo.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Histone Deacetylase Inhibitors Modulate the Transcriptional Regulation of Guanylyl Cyclase/Natriuretic Peptide Receptor-A Gene

Kumar

Tripathi

Pandey

2014

Journal of Biological Chemistry

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“…Overexpression of Ets-1 in mouse mesangial cells increases NPR-A gene transcription 12-fold, whereas overexpression of GATA-1 or Lyf-1 results in a 50% and 80% reduction in promoter activity, respectively. 68 Mutation or deletion of the c-Ets binding elements positioned at approximately Ϫ45 and Ϫ14 in the murine gene leads to a loss of the Ets-1-dependent induction. 68 A series of Sp1 sites positioned between Ϫ118 and Ϫ83 in the human NPR-B gene play a dominant role in the regulation of that gene's basal promoter activity.…”

Section: Regulation Of the Np Receptorsmentioning

confidence: 99%

Molecular Biology of the Natriuretic Peptide System

et al. 2007

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T he natriuretic peptides (NPs) are a group of peptide hormones that play important roles in the control of renal, cardiovascular, endocrine, and skeletal homeostasis. Atrial NP (ANP) was first identified as an activity by de Bold et al 1 in 1981. It is a 28 amino acid peptide in humans that assumes a hairpin structure by virtue of a cystine bridge that links residues 7 and 23 ( Figure 1). Brain NP (BNP), also known as the B-type NP, is 32 amino acids long in the human. It has a similar hairpin structure but demonstrates considerably more heterogeneity across species than ANP. C-type NP (CNP) is a 22 amino acid peptide that has a truncated carboxy terminus beyond the second cystine residue in the bridge.ANP and BNP are produced primarily within the muscle cells of the heart. ANP shows a preference for expression in the cardiac atria versus ventricle, whereas BNP is more equivalently expressed throughout the heart. ANP is also expressed in the hypothalamus where it is thought to control blood pressure (BP), sympathetic outflow, vasopressin secretion, drinking behavior, and cardiovascular homeostasis. BNP, on the other hand, is expressed in the brains of only a few species (eg, pig and dog), where its function remains unknown. CNP is expressed in the central nervous system, reproductive tract, bone, and endothelium of blood vessels.There are 3 different types of NP receptors, and each of them spans the membrane bilayer as a single transmembrane segment. The type A NP receptor (NPR-A) is also known as the particulate guanylyl cyclase A. It is the high affinity receptor for both ANP and BNP. A schematic of the structure of this receptor is presented in Figure 2. NPR-A has a glycosylated, extracellular, ligand-binding domain linked to a hydrophobic transmembrane spanning segment, a noncatalytic, ATP-binding, kinase-like domain in the proximal intracellular portion of the molecule, which is thought to function as a regulator of receptor activity, and a short hinge region. The NPR-A carboxy terminus contains the particulate guanylyl cyclase that is the catalytic effector of the receptor. Association of NPR-A with its cognate ligand (ANP or BNP) causes a conformational change in the kinase-like domain, which relaxes tonic inhibition of guanylyl cyclase activity and increases production of cGMP. NPR-B shares a similar structure with NPR-A. It binds selectively to CNP. NPR-C, the so-called clearance receptor, has an extracellular domain that is structurally homologous to that of the other NPRs. This is linked to a single transmembrane-spanning segment followed by an intracellular domain containing only 37 amino acids. NPR-C binds with high affinity to all 3 NPs, as well as to a variety of other peptides with more distant structural homology. The primary role of NPR-C is to function in a clearance mode, capturing and degrading NPs in the extracellular compartment. 2 Earlier reviews have dealt with the regulators of NP gene expression. 3 This brief review will focus on the molecular details underlying the transcriptional re...

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Central role of guanylyl cyclase in natriuretic peptide signaling in hypertension and metabolic syndrome

2009

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Studied for nearly 30 years for its ability to control many parameters, such as vascular smooth muscle cell relaxation, heart fibrosis, and kidney function, the natriuretic peptide (NP) system is now considered to be a key element in several other major metabolic pathways. After stimulation by NPs, natriuretic peptide receptors (NPR) convert GTP to the second messenger cGMP. In addition to its vasodilatory effects and natriuretic and diuretic functions, cGMP has been positively associated with fat cell function, apoptosis, and NPR expression/activity modulation. The NP system is also closely linked to metabolic syndrome (MetS) progression and obesity control. A new era is now on its way targeting the NP system to not only treat high blood pressure, but to also assist in the fight against the obesity pandemic. Here, we summarize recent data on the role of NPs in hypertension and MetS.

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Transcriptional regulation of guanylyl cyclase/natriuretic peptide receptor-A gene

Cited by 11 publications

References 38 publications

Histone Deacetylase Inhibitors Modulate the Transcriptional Regulation of Guanylyl Cyclase/Natriuretic Peptide Receptor-A Gene

Histone Deacetylase Inhibitors Modulate the Transcriptional Regulation of Guanylyl Cyclase/Natriuretic Peptide Receptor-A Gene

Molecular Biology of the Natriuretic Peptide System

Central role of guanylyl cyclase in natriuretic peptide signaling in hypertension and metabolic syndrome

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