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Vasopressin Receptors (vasopressin + receptor)

Distribution by Scientific Domains
Medical Sciences73%
Chemistry20%

Terms modified by Vasopressin Receptors

  • vasopressin receptor antagonist
    		•

    Selected Abstracts

    Expression of the Genes Encoding the Vasopressin-Activated Calcium-Mobilizing Receptor and the Dual Angiotensin II/Vasopressin Receptor in the Rat Central Nervous System

    JOURNAL OF NEUROENDOCRINOLOGY, Issue 7 2000
    Hurbin
    The distributions of two newly discovered receptors, the vasopressin-activated calcium-mobilizing receptor (VACM-1) and the dual angiotensin II/vasopressin receptor (AII/AVP), in the central nervous system (CNS) of the rat were determined using reverse transcriptase-polymerase chain reaction and in situ hybridization. The sequence of the rat VACM-1 cDNA was determined and found very homologous to the rabbit and human sequences. Both VACM-1 and AII/AVP receptor genes were widely expressed in the brain, but differed according to the cell type studied. Glial cells were very faintly labelled. The epithelial cells of the choroid plexuses, the ependymal cells and the pia mater were all labelled. Both genes were most active in neurones throughout the CNS. VACM-1 and AII/AVP receptors were detected in neurones previously shown to possess V1a and V1b vasopressin receptors, and/or the AT1 and AT2 angiotensin II receptors in many brain areas. This was the case for the magnocellular neurones of the supraoptic and paraventricular nuclei of the hypothalamus. We suggest that the VACM-1 and AII/AVP receptors may account for the V2 -like responses to vasopressin by these neurones which lack a genuine V2 vasopressin receptor. [source]

    Ageing and the Diurnal Expression of the mRNAs for Vasopressin and for the V1a and V1b Vasopressin Receptors in the Suprachiasmatic Nucleus of Male Rats

    JOURNAL OF NEUROENDOCRINOLOGY, Issue 6 2004
    T. Kalamatianos
    Abstract Changes in the function of neuropeptide synthesizing cells within the suprachiasmatic nucleus (SCN), the site of the predominant circadian pacemaker, may underlie the disturbance of rhythms observed during ageing. Arginine vasopressin (AVP) is synthesized by nearly one-third of SCN neurones in the rat. This peptide has predominantly excitatory actions within the SCN mediated by V1 -type receptors; the extent to which the V1a and/or V1b receptor subtypes are involved in SCN functions remains to be determined. The present study used isotopic in situ hybridization histochemistry to examine the effects of ageing on expression of mRNAs for AVP and V1a in the SCN and for V1b in the SCN and supraoptic nucleus (SON) of male rats kept under a 12 : 12 h light/dark cycle. Analysis of film autoradiographs from young adult (2,3-month-old; n = 40) or aged (19,20-month-old; n = 40) animals, at eight time points across the light/dark cycle, revealed an equivalent pattern and amplitude for the diurnal rhythm of AVP mRNA in the SCN of the young adult and aged groups. Both groups also displayed a significant diurnal rhythm in the expression of V1a receptor mRNA; however, the amplitude of this rhythm was reduced in the aged group, due to increased levels during the light phase and early part of night. Although the expression of V1b mRNA did not display a significant diurnal rhythm within the SCN or SON, persistently elevated levels for V1b mRNA were observed in the aged group at both sites. [source]

    Evaluation of detergents for the soluble expression of ,-helical and ,-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system

    FEBS JOURNAL, Issue 23 2005
    Christian Klammt
    Cell-free expression has become a highly promising tool for the fast and efficient production of integral membrane proteins. The proteins can be produced as precipitates that solubilize in mild detergents usually without any prior denaturation sttif. Alternatively, membrane proteins can be synthesized in a soluble form by adding detergents to the cell-free system. However, the effects of a representative variety of detergents on the production, solubility and activity of a wider range of membrane proteins upon cell-free expression are currently unknown. We therefore analyzed the cell-free expression of three structurally very different membrane proteins, namely the bacterial ,-helical multidrug transporter, EmrE, the ,-barrel nucleoside transporter, Tsx, and the porcine vasopressin receptor of the eukaryotic superfamily of G-protein coupled receptors. All three membrane proteins could be produced in amounts of several mg per one ml of reaction mixture. In general, the detergent 1-myristoyl-2-hydroxy- sn -glycero-3-[phospho- rac -(1-glycerol)] was found to be most effective for the resolubilization of membrane protein precipitates, while long chain polyoxyethylene-alkyl-ethers proved to be most suitable for the soluble expression of all three types of membrane proteins. The yield of soluble expressed membrane protein remained relatively stable above a certain threshold concentration of the detergents. We report, for the first time, the high-level cell-free expression of a ,-barrel type membrane protein in a functional form. Structural and functional variations of the analyzed membrane proteins are evident that correspond with the mode of expression and that depend on the supplied detergent. [source]

    Expression of the Genes Encoding the Vasopressin-Activated Calcium-Mobilizing Receptor and the Dual Angiotensin II/Vasopressin Receptor in the Rat Central Nervous System

    JOURNAL OF NEUROENDOCRINOLOGY, Issue 7 2000
    Hurbin
    The distributions of two newly discovered receptors, the vasopressin-activated calcium-mobilizing receptor (VACM-1) and the dual angiotensin II/vasopressin receptor (AII/AVP), in the central nervous system (CNS) of the rat were determined using reverse transcriptase-polymerase chain reaction and in situ hybridization. The sequence of the rat VACM-1 cDNA was determined and found very homologous to the rabbit and human sequences. Both VACM-1 and AII/AVP receptor genes were widely expressed in the brain, but differed according to the cell type studied. Glial cells were very faintly labelled. The epithelial cells of the choroid plexuses, the ependymal cells and the pia mater were all labelled. Both genes were most active in neurones throughout the CNS. VACM-1 and AII/AVP receptors were detected in neurones previously shown to possess V1a and V1b vasopressin receptors, and/or the AT1 and AT2 angiotensin II receptors in many brain areas. This was the case for the magnocellular neurones of the supraoptic and paraventricular nuclei of the hypothalamus. We suggest that the VACM-1 and AII/AVP receptors may account for the V2 -like responses to vasopressin by these neurones which lack a genuine V2 vasopressin receptor. [source]

    AL-3138 Antagonizes FP Prostanoid Receptor-mediated Inositol Phosphates Generation: Comparison with Some Purported FP Antagonists

    JOURNAL OF PHARMACY AND PHARMACOLOGY: AN INTERNATI ONAL JOURNAL OF PHARMACEUTICAL SCIENCE, Issue 12 2000
    N. A. SHARIF
    The aim of this study was to pharmacologically characterize the antagonist properties of a novel prostaglandin F2, (PGF2,) analogue (11-deoxy-16-fluoro PGF2,; AL-3138) using a variety of second-messenger assays of prostaglandin receptor subtypes. A detailed comparison was made between AL-3138 and some purported FP receptor antagonists such as PGF2, dimethylamine, PGF2, dimethylamide, glibenclamide and phloretin using the FP receptor-mediated phosphoinositide turnover assay in A7r5 rat thoracic aorta smooth muscle cells and mouse Swiss 3T3 fibroblasts. The potency and efficacy of AL-3138 as an FP receptor agonist were: EC50 = 72.2 ± 17.9 nM (Emax = 37%) (n = 3) in A7r5 cells and EC50 = 20.5 ± 2.8 nM (Emax = 33%) (n = 5) in 3T3 cells. Being a partial agonist, the antagonist potency of AL-3138 against fluprostenol in A7r5 cells was determined to be: Ki = 296 ± 17 nM (n = 3) and Kb = 182 ± 44nM (n = 5) (-log Kb = 6.79 ± 0.1). AL-3138 exhibited very minimal or no antagonistic effects at EP2, EP4, DP and TP prostaglandin receptors. Both PGF2, dimethylamide and PGF2, dimethylamine were inactive as FP receptor antagonists, whereas phloretin and glibenclamide were very weak and had -log Kb values of 5.28 ± 0.09 (n = 3) and 3.58 ± 0.32 (n = 3), respectively. However, phloretin antagonized functional responses of EP2 and DP prostanoid receptors, and also the V1 , vasopressin receptor. AL-3138 competed for [3H]PGF2, binding to FP receptors with a relatively high affinity (IC50high = 312 ± 95nM) matching its functional antagonist potency. In conclusion, AL-3138 is a more potent and selective FP receptor antagonist than glibenclamide, phloretin, PGF2, dimethylamide and PGF2, dimethylamine and is therefore a unique and novel pharmacological tool to help characterize FP receptor-mediated functions. [source]

    A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2005
    Syed Saad Mahmood
    The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor (GPCR) involved in the regulation of body-fluid osmolality, blood volume and blood pressure. Signal transduction is mediated by the third intracellular loop of this seven-transmembrane protein as well as by the C-terminal cytoplasmic segment. A chimera of the maltose-binding protein (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P21, with unit-cell parameters a = 51.10, b = 66.56, c = 115.72,Ĺ, , = 95.99°. The 1.8,Ĺ crystal structure reveals the conformation of MBP and part of the linker region of this chimera, with the C-terminal segment being unstructured. This may reflect a conformational plasticity in the C-­terminal segment that may be necessary for proper function of V1R. [source]

    Vasopressin modulates lateral septal network activity via two distinct electrophysiological mechanisms

    EUROPEAN JOURNAL OF NEUROSCIENCE, Issue 9 2007
    G. Allaman-Exertier
    Abstract The lateral septal area is rich in vasopressin V1A receptors and is densely innervated by vasopressinergic axons, originating mainly from the bed nucleus of the stria terminalis and the amygdala. Genetic and behavioral studies provide evidence that activation of vasopressin receptors in this area plays a determinant role in promoting social recognition. What could be the neuronal mechanism underlying this effect? Using rat brain slices and whole-cell recordings, we found that lateral septal neurons are under the influence of a basal GABAergic inhibitory input. Vasopressin, acting via V1A but not V1B receptors, greatly enhanced this input in nearly all neurons. The peptide had no effect on miniature inhibitory postsynaptic currents, indicating that it acted on receptors located in the somatodendritic membrane, rather than on axon terminals, of GABAergic interneurons. Cell-attached recordings showed that vasopressin can cause a direct excitation of a subpopulation of lateral septal neurons by acting via V1A but not V1B receptors. The presence in the lateral septum of V1A but not of V1B receptors was confirmed by competition binding studies using light microscopic autoradiography. In conclusion, vasopressin appears to act in the lateral septum in a dual mode: (i) by causing a direct excitation of a subpopulation of neurons, and (ii) by causing an indirect inhibition of virtually all lateral septal neurons. This modulation by vasopressin of the lateral septal circuitry may be part of the neuronal mechanism by which the peptide, acting via V1A receptors, promotes social recognition. [source]

    Naturally Occurring Differences in Maternal Care are Associated with the Expression of Oxytocin and Vasopressin (V1a) Receptors: Gender Differences

    JOURNAL OF NEUROENDOCRINOLOGY, Issue 5 2002
    D. D. Francis
    Abstract Variations in maternal care have been associated with long-term changes in neurochemistry and behaviour in adult rats. Rats receiving high levels of licking and grooming as pups are less fearful and more maternal than rats receiving low levels of maternal licking and grooming. Central pathways for oxytocin and vasopressin have been implicated in the neurobiology of anxiety and social behaviours. We assessed whether variations in maternal care were associated with differences in oxytocin receptors (OTR) or vasopressin (V1a) receptors in the brains of adult offspring. In the central nucleus of the amygdala and bed nucleus of the stria terminalis, OTR binding was increased in adult females, but not adult males, that had received high levels of maternal licking and grooming as pups. Conversely, amygdala V1a receptor binding was increased in males, but not females, that had received high levels of maternal licking and grooming. These findings suggest that variations in maternal care may influence the expression of oxytocin and vasopressin receptors in a gender-specific manner. [source]

    Expression of the Genes Encoding the Vasopressin-Activated Calcium-Mobilizing Receptor and the Dual Angiotensin II/Vasopressin Receptor in the Rat Central Nervous System

    JOURNAL OF NEUROENDOCRINOLOGY, Issue 7 2000
    Hurbin
    The distributions of two newly discovered receptors, the vasopressin-activated calcium-mobilizing receptor (VACM-1) and the dual angiotensin II/vasopressin receptor (AII/AVP), in the central nervous system (CNS) of the rat were determined using reverse transcriptase-polymerase chain reaction and in situ hybridization. The sequence of the rat VACM-1 cDNA was determined and found very homologous to the rabbit and human sequences. Both VACM-1 and AII/AVP receptor genes were widely expressed in the brain, but differed according to the cell type studied. Glial cells were very faintly labelled. The epithelial cells of the choroid plexuses, the ependymal cells and the pia mater were all labelled. Both genes were most active in neurones throughout the CNS. VACM-1 and AII/AVP receptors were detected in neurones previously shown to possess V1a and V1b vasopressin receptors, and/or the AT1 and AT2 angiotensin II receptors in many brain areas. This was the case for the magnocellular neurones of the supraoptic and paraventricular nuclei of the hypothalamus. We suggest that the VACM-1 and AII/AVP receptors may account for the V2 -like responses to vasopressin by these neurones which lack a genuine V2 vasopressin receptor. [source]

    Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptors,molecular dynamics study of the activated receptor,vasopressin,G, systems

    JOURNAL OF PEPTIDE SCIENCE, Issue 3 2006
    Magdalena J., lusarz
    Abstract Vasopressin (CYFQNCPRG-NH2, 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,C -terminal peptide of transducin MII-Gt(338-350) prototype as a template. AVP was docked into the receptor-G, systems. The three lowest-energy pairs of receptor-AVP-G, (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, 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. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd. [source]

    Vasopressin receptor antagonists: pharmacological tools and potential therapeutic agents

    AUTONOMIC & AUTACOID PHARMACOLOGY, Issue 2 2006
    J. O. Streefkerk
    Summary 1 The present survey deals with the development and applications of non-peptidergic vasopressin receptor antagonists. 2 The existence of at least three vasopressin receptors (V1, V2 and V3 respectively) is firmly established. 3 V1 -receptors play a relevant role in the regulation of vascular tone, whereas V2 -receptors are known to mediate the antidiuretic activity of vasopressin at the level of the renal collecting ducts. The V3 -receptor appears to be involved in the release of the adreno-corticotropic hormone. 4 Vasopressin receptor antagonists which are peptides have been known for several decades, more recently, both V1 - and V2 -receptor blockers which are non-peptidergic have been introduced, as well as agents with affinity for both V1 - and V2 -receptor subtypes. A survey of these non-peptidergic antagonists is presented here. Such compounds are useful as pharmacological tools, and they can also be thought of as therapeutic agents as therapeutic agents in cardiovascular and renal diseases. 5 Selective V1 - and V2 -receptor antagonists were used to study the interaction between vasopressin receptors and sympathetic neurones. Depending on the experimental model used this interaction can occur at either the pre- or postsynaptic sites. In both cases predominantly V1 -receptors are involved. 6 A brief survey is given of the potential use of V-receptor antagonists in the drug therapy of syndrome of inappropriate antidiuretic hormone secretion and other water retaining disorders, congestive heart failure and certain forms of hypertension (in particular in the Negroid hypertensive patients). [source]

    Pharmacological characterization of F-180: a selective human V1a vasopressin receptor agonist of high affinity

    BRITISH JOURNAL OF PHARMACOLOGY, Issue 7 2002
    Miriam Andrés
    The pharmacological properties of F-180, a vasopressin (VP) structural analogue, were determined on CHO cells expressing the different human vasopressin and oxytocin (OT) receptor subtypes. Binding experiments revealed that F-180 exhibited a high affinity for the human V1a receptor subtype (Ki=11 nM) and was selective for this receptor subtype. Functional studies performed on CHO cells expressing human V1a receptors indicate that similarly to AVP, F-180 can stimulate the accumulation of inositol phosphate. The activation constant (Kact) for both F-180 and AVP was 1.7 nM. F-180 was also an agonist for the human V2 and V1b receptor subtypes and an antagonist for the human OT receptor. Since marked species pharmacological differences for vasopressin receptors have been described, we studied the properties of F-180 on various mammalian species. F-180 showed high affinity and good selectivity for human and bovine V1a receptors, but weak affinity and non selective properties for rat V1a receptors. To assess the functional properties of F-180 on a native biological model, we performed studies on primary cultures of cells from bovine zona fasciculata (ZF). As AVP, F-180 stimulated inositol phosphate accumulation and cortisol secretion with similar efficiency. In conclusion, we demonstrate that F-180 is the first selective V1a agonist described for human and bovine vasopressin receptors. Therefore F-180 can be used as a powerful pharmacological tool to characterize the actions of vasopressin that are mediated by V1a receptor subtypes. British Journal of Pharmacology (2002) 135, 1828,1836; doi:10.1038/sj.bjp.0704634 [source]

    Hyponatremia and Vasopressin Antagonism in Congestive Heart Failure

    CLINICAL CARDIOLOGY, Issue 11 2007
    Siva Kumar M.D
    Abstract In a national heart failure registry, hyponatremia (serum sodium < 130 mEq/L) was initially reported in 5% of patients and considered a risk factor for increased morbidity and mortality. In a chronic heart failure study, serum sodium level on admission predicted an increased length of stay for cardiovascular causes and increased mortality within 60 days of discharge. Hyponatremia in patients with congestive heart failure (CHF) is associated with a higher mortality rate. Also, by monitoring and increasing serum sodium levels during hospitalization for CHF, patient outcomes may improve. This review describes the pathophysiology of hyponatremia in relation to CHF, including the mechanism of action of vasopressin receptors in the kidney, and assesses the preclinical and clinical trials of vasopressin receptor antagonists,agents recently developed to treat hyponatremia. In hospitalized patients with CHF, hyponatremia plays a major role in poor outcomes. Vasopressin receptor antagonists have been shown to be safe and effective in clinical trials in patients with hyponatremia. Copyright © 2007 Wiley Periodicals, Inc. [source]