Renal Actions of Vasopressin

Knepper, Mark A.; Valtin, Heinz; Sands, Jeff M.

doi:10.1002/cphy.cp070313

Cited by 10 publications

(7 citation statements)

References 214 publications

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“…1985)] are sites of long‐term regulation of abundance of the respective apical Na transport protein (BSC1/NKCC2 in the thick ascending limb and ENaC in the collecting duct). The pattern of response seen also matches the known localization of V2 vasopressin receptors in the thick ascending limb and collecting duct (Knepper et al . 2000).…”

Section: Typical Resultssupporting

confidence: 83%

Targeted proteomics in the kidney using ensembles of antibodies

Knepper

Masilamani

2001

Acta Physiologica Scandinavica

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Building on extensive physiological characterization of sodium transport mechanisms along the renal tubule over the past 30 years, complementary DNAs for almost all of the major transporters and channels responsible for renal tubular sodium reabsorption have been cloned over the past 10 years. The consequence is the generation of a broad range of cDNA and antibody probes which can be used to investigate physiological mechanisms on a molecular level. An ensemble of such probes can be exploited for comprehensive analysis of integrative physiological processes, approaches which are referred to as 'physiological genomics' or 'physiological proteomics'. In this review, we describe a targeted proteomic approach to comprehensive analysis of sodium transporter and water channel protein abundance along the renal tubule using an ensemble of rabbit polyclonal antibodies directed to the major sodium transporters and water channels expressed in each renal tubule segment. We discuss preparation and characterization of the antibodies, strategies for quantification of transporter protein abundance, and provide examples of the application of antibody-based targeted proteomics analysis of kidney tissue, revealing the effects of elevations of circulating aldosterone levels and circulating vasopressin levels on sodium transporter, sodium channel, and water channel abundance in kidney.

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Section: Typical Resultssupporting

confidence: 83%

Targeted proteomics in the kidney using ensembles of antibodies

Knepper

Masilamani

2001

Acta Physiologica Scandinavica

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“…In contrast, renal tubule epithelia with very low water permeabilities (thin ascending limb, thick ascending limb and distal convoluted tubules) do not appear to express aquaporins. The terminal part of the renal tubule, the connecting tubules and collecting ducts have variable water permeability that is controlled by the peptide hormone vasopressin [5]. This renal tubule segment expresses three aquaporins: aquaporin 2 (AQP2) in the apical plasma membrane [6] and aquaporin 3 and 4 (AQP3 and AQP4) in the basolateral plasma membrane [7] [8].…”

Section: Introductionmentioning

confidence: 99%

Vasopressin and the regulation of aquaporin-2

2013

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Water excretion is regulated in large part through the regulation of the osmotic water permeability of the renal collecting duct epithelium. The water permeability is controlled by vasopressin through regulation of the water channel, aquaporin-2 (AQP2). Two processes contribute: 1) regulation of AQP2 trafficking to the apical plasma membrane; and 2) regulation of the total amount of the AQP2 protein in the cells. Regulation of AQP2 abundance is defective in several water balance disorders including many polyuric disorders and the syndrome of inappropriate antidiuresis (SIADH). Here we review vasopressin signaling in the renal collecting duct that is relevant to the two modes of water permeability regulation.

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“…V1aR, located in the vascular smooth muscle are responsible mainly for increase of blood pressure and mediation of remaining physiological functions of AVP [9,10], with the exception of those mediated via V1bR and V2R. The latter is found in the collecting duct (CD) of the kidney, where it mediates the antidiuretic effect of vasopressin: water reabsorption and concentration of the urine [11,12]. The V1b (also termed V3) pituitary receptor, not a subject of this work, controls adrenocorticotropin hormone (ACTH) secretion and AVP actions in the central nervous system [13,14].…”

Section: Introductionmentioning

confidence: 99%

Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptors—molecular dynamics study of the activated receptor–vasopressin–Gα systems

et al. 2006

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Vasopressin (CYFQNCPRG-NH(2), AVP) is a semicyclic endogenous peptide, which exerts a variety of biological effects in mammals. The main physiological roles of AVP are the regulation of water balance and the control of blood pressure and adrenocorticotropin hormone (ACTH) secretion, mediated via three different subtypes of vasopressin receptors: V1a, V1b and V2 receptors (V1aR, V1bR and V2R, respectively). They are the members of the class A, G-protein-coupled receptors (GPCRs). AVP also modulates several behavioral and social functions. In this study, the interactions responsible for AVP binding to vasopressin V1a and V2 receptors versus the closely related oxytocin ([I3,L8]AVP, OT) receptor (OTR) have been investigated. Three-dimensional models of the activated receptors were constructed using multiple sequence alignment, followed by homology modeling using the complex of activated rhodopsin with Gt(alpha) C-terminal peptide of transducin MII-Gt(338-350) prototype as a template. AVP was docked into the receptor-G(alpha) systems. The three lowest-energy pairs of receptor-AVP-G(alpha) (two complexes per each receptor) were selected. The 1-ns unconstrained molecular dynamics (MD) of complexes embedded into the fully hydrated 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) lipid bilayer was conducted in the AMBER 7.0 force field. Six relaxed receptor-AVP-G(alpha) models were obtained. The residues responsible for AVP binding to vasopressin receptors have been identified and a different mechanism of AVP binding to V2R than to V1aR has been proposed.

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Renal Actions of Vasopressin

Cited by 10 publications

References 214 publications

Targeted proteomics in the kidney using ensembles of antibodies

Targeted proteomics in the kidney using ensembles of antibodies

Vasopressin and the regulation of aquaporin-2

Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptors—molecular dynamics study of the activated receptor–vasopressin–Gα systems

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