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Effect of dDAVP on outer medullary gene expression in Brattleboro rats

ABSTRACT: Activation of the renal urine concentrating mechanism by vasopressin requires the coordinated regulation of multiple gene products including ion transporters, and water channels as well as regulatory proteins like protein kinases and phosphatases or enzymes involved in the energy-metabolism of the cells. We used microarray analysis of AVP-regulated gene products in a rat model of central diabetes insipidus (DI) to generate a comprehensive database documenting these changes.

ORGANISM(S): Rattus norvegicus

PROVIDER: GSE34225 | GEO | 2012/03/01

SECONDARY ACCESSION(S): PRJNA149779

REPOSITORIES: GEO

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Effect of dDAVP on outer medullary gene expression in Brattleboro rats

Project description:Activation of the renal urine concentrating mechanism by vasopressin requires the coordinated regulation of multiple gene products including ion transporters, and water channels as well as regulatory proteins like protein kinases and phosphatases or enzymes involved in the energy-metabolism of the cells. We used microarray analysis of AVP-regulated gene products in a rat model of central diabetes insipidus (DI) to generate a comprehensive database documenting these changes. For microarray studies young (8 weeks) adult male Brattleboro rats were randomly divided into 2 groups (n = 3 per group) and treated for 3 days with either 1-desamino-8-D-Arg vasopressin (dDAVP; 5ng/h; Sigma Aldrich, Germany) or vehicle via osmotic minipump (ALZET minipump model 2001, Charles River, Sulzfeld, Germany). At the end of the treatment period animals were sacrificed and the kidneys removed. The outer medulla was isolated and used for cDNA generation and subsequent microarray analysis using [Rat230_2] Affymetrix Rat Genome 230 2.0 Array.

2012-03-01 | E-GEOD-34225 | biostudies-arrayexpress

Vasopressin (AVP) and the V2R specific agonist dDAVP 7 day infusion into Aquaporin 1 knockout animals

Project description:Vasopressin, the antidiuretic hormone, acts on the renal collecting duct. In this experiment both vasopressin (AVP) and the V2R specific agonist dDAVP were infused into Aquaporin 1 knockout animals for 7 days. The aim of the experiment was to identify genes increased by vasopressin receptors in the renal medullary collecting ducts, in the absence of an increase in renal medullary osmolarity (the AQP1 knockouts are concentrating mechanism knockouts). All experiments used inner medulla tissue for the RNA isolation. Hybridizations were performed that compared kidney inner medulla total RNA from three control mice against kidney medulla total RNA from 3 mice infused with either arginine vasopressin (AVP) or des-amino-D-arginine vasopressin (dDAVP).

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Vasopressin (AVP) and the V2R specific agonist dDAVP 7 day infusion into Aquaporin 1 knockout animals

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Arginine vasopressin infusion is sufficient to model preeclampsia in mice

Project description:Copeptin, the c-terminal fragment of arginine vasopressin (AVP), is considered a useful biomarker for the secretion of AVP. Preeclampsia, a cardiovascular disorder of pregnancy, has been associated with elevated maternal plasma copeptin concentrations. These findings led us to hypothesize that AVP secretion is elevated during preeclampsia, and may contribute to the pathogenesis of this disorder. To examine the effect of increased circulating AVP upon placental development, exogenous AVP was infused into pregnant wildtype C57BL/6J mice, and the transcriptome of a single placenta per dam was assessed at gestational day 12.5 by RNAseq.

2022-05-28 | GSE116751 | GEO

Transcriptome changes in response to dDAVP stimulation in CRISPR/Cas9 mediated Camk2d knock-out mpkCCD cells

Project description:The Ca2+/CaM-dependent protein kinase 2-delta (CAMK2D) has been proposed to be involved in vasopressin signaling in the renal collecting duct, which controls water and salt excretion by the kidney. RNA sequancing and quantitative proteomics analyses identified the expression of multiple CAMK2 isoforms, with CAMK2D being the most abundant in collecting duct cells. To investigate the role of CAMK2D in regulating RNA expression in response to vasopressin signaling, the transcriptome of CRISPR/Cas9-mediated Camk2d knock-out mpkCCD cells was profiled using RNA-Seq in the presence of vasopressin analogue dDAVP.

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Expression data from mouse collecting duct cell, mpkCCD, in response to a peptide hormone vasopressin analog, dDAVP

2010-12-09 | GSE19938 | GEO

Expression data from mouse collecting duct cell, mpkCCD, in response to a peptide hormone vasopressin analog, dDAVP

Project description:Vasopressin is the major hormone that regulates renal water excretion. It does so by binding to a receptor in renal collecting duct cells, triggering signaling pathways that ultimately regulate the abundance, location, and activity of the water channel protein aquaporin 2. We took an advantage of quantitative large scale proteomic technologies and oligonucleotide microarrays to quantify steady state changes in protein and transcript abundances in response to vasopressin in a collecting duct cell line, mpkCCD clone 11 (Yu et al. PNAS 2009, 106:2441-2446). This cell line originally developed by Alan Vandewalle’s group recapitulates vasopressin-mediated AQP2 expression and phosphorylation as seen in native colleting duct cells. The mpkCCD cells were grown on membrane supports to permit polarization. Once transepithelial resistance reached 5kohm per centimeter square and higher, the cells were exposed to the vasopressin V2 receptor analog, dDAVP, at a physiological concentration, 0.1nM, for 5 days. Control experiments were done with cells exposed to vehicle alone. Total RNA was harvested and processed for transcript expression analysis using Affymetrix GeneChip Mouse Genome 430 2.0 Arrays. Each experimental treatment, vehicle and dDAVP, was repeated 3 times.

2010-12-09 | E-GEOD-19938 | biostudies-arrayexpress

Vasopressin V2 Receptor, Tolvaptan, and ERK1/2 Phosphorylation in the Renal Collecting Duct II

Project description:Activation of ERK1 and ERK2 is essential in regulation of a wide variety of cellular and physiological processes. In native inner medullary collecting ducts, vasopressin (AVP) working through the V2 subtype vasopressin receptor (V2R)-mediated activation of Gαs, inhibits ERK1 and ERK2 activity. However, it has been reported that V2R can signal independently of Gαs through the activation of β-arrestin, which activates ERK1 and ERK2. Vaptans, V2R antagonists that function as so-called “inverse agonists”, have the potential of promoting cell proliferation via β-arrestin-dependent ERK activation. Here we use the mpkCCD cell line which natively expresses V2R to investigate the effects of AVP, the V2-selective analog dDAVP, and tolvaptan on ERK1 and ERK2 phosphorylation and activation. We demonstrated that ERK1 and ERK2 phosphorylation in mpkCCD cells was significantly reduced by either AVP or dDAVP, in contrast to the increases seen in non-collecting duct cells overexpressing V2R. We also found that tolvaptan has a strong effect to increase ERK1 and ERK2 phosphorylation in the presence of dDAVP and that the tolvaptan effect to increase ERK1 and ERK2 phosphorylation is absent in PKA-null mpkCCD cells. Thus, it appears that the tolvaptan effect to increase ERK activation is PKA-dependent and, therefore, not mediated by the β-arrestin pathway. Overall, the studies show that AVP decreases and that tolvaptan increases ERK1 and ERK2 activation in cells expressing V2R at endogenous levels, and provide no evidence for a role for β-arrestin in the regulation of ERK1 and ERK2 activity.

2023-11-17 | GSE243773 | GEO

Comprehensive Proteomic Profiling of Nuclear Fractions from Native Renal Inner Medullary Collecting Duct Cells

Project description:Regulation of renal water excretion is dependent on control of the molecular water channel aquaporin‐2 by the peptide hormone vasopressin in renal collecting duct cells. The control is in part due to the regulation of transcription of the Aqp2 gene and other genes by vasopressin. A systems biology‐based approach to understanding transcriptional control in renal collecting duct cells depends on knowledge of what transcription factors and other regulatory proteins are present in the cells' nucleus. The goal of this paper is to report comprehensive proteomic profiling of nuclear proteins in native inner medullary collecting duct (IMCD) cells of the rat. Multi‐dimensional separation procedures and state‐of‐the art protein mass spectrometry allowed the high stringency identification of a total of 5105 proteins in nuclear pellet (NP) and nuclear extract (NE) fractions of biochemically isolated rat IMCD cells (URL: https://helixweb.nih.gov/ESBL/Database/IMCD_Nucleus/)*. The analysis identified 369 transcription factor proteins out of the 1371 transcription factors coded by the rat genome. The analysis added 1898 proteins to the recognized proteome of rat IMCD cells, now amounting to 7003 unique proteins. Analysis of samples treated with the vasopressin analog dDAVP (1 nM for 30min) or its vehicle revealed 99 proteins in the NP fraction and 88 proteins in the NE fraction with significant changes in spectral counts (Fisher Exact Test, P<0.005). Among those altered by vasopressin were 7 distinct histone proteins all of which showed decreased abundance in the NP fraction, consistent with a possible effect of vasopressin to induce chromatin remodeling.

2018-10-24 | PXD002680 | Pride