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      Historadioautographic Localization of Oxytocin and V1a Vasopressin Binding Sites in the Kidney of Developing and Adult Rabbit, Mouse and Merione and of Adult Human

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          Abstract

          The localization of oxytocin (OT) binding sites and vasopressin (VP) binding sites of the V1a subtype was investigated by radioautography in kidneys of rabbits, mice and meriones during postnatal development and in the adult, and in the human kidney. Kidney sections were incubated in the presence of selective radioiodinated OT and V1a antagonists, respectively. The localizations were compared with those previously described in the rat. The main finding of the study was the almost constant presence in the cortex of V1a binding sites in the connecting tubule, the cortical collecting duct and in the juxtaglomerular apparatus (on the intra- and extraglomerular mesangium and the afferent arteriole). This distribution suggests an interaction of VP via V1a receptors and the kallikrein-kinin system in the kidney. OT binding sites, in comparison with V1a binding sites, were fewer and less constantly detectable in the kidney of the different species. In the mouse, their presence on the limbs of Henle’s loop in the medulla points to the possibility of their involvement in the medullary concentrating process. In the kidneys of the various species, OT and V1a binding sites occurred always in differential structures. In contrast, in the human kidney cortex, a colocalization of OT and V1a binding sites was almost constantly observed. This raises the question as to the specificity of the neurohypophysial hormone receptors in the human kidney.

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          Most cited references 7

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          Cloning and characterization of a vasopressin V2 receptor and possible link to nephrogenic diabetes insipidus.

          The antidiuretic effect of arginine vasopressin (AVP) is mediated by renal-type (V2) receptors linked to adenylyl cyclase. We report here the cloning of the rat kidney V2 AVP receptor complementary DNA that encodes a 370-amino-acid protein with a transmembrane topography characteristic of G protein-coupled receptors, and with similarity to the V1a (hepatic) AVP receptor in its seven membrane-spanning domains. Expression of the cloned cDNA in mammalian cells showed specific ligand binding and activity characteristic of the native V2 AVP receptor. The receptor messenger RNA is detected only in the kidney. The human V2 receptor gene has been localized to the long arm of the X chromosome close to the locus for nephrogenic diabetes insipidus, an X-linked recessive disorder characterized by renal resistance to the antidiuretic action of AVP.
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            Molecular cloning and expression of a rat V1a arginine vasopressin receptor.

            The neurohypophyseal hormone arginine vasopressin has diverse actions, including the inhibition of diuresis, contraction of smooth muscle, stimulation of liver glycogenolysis and modulation of adrenocorticotropic hormone release from the pituitary. Arginine vasopressin receptors are G protein-coupled and have been divided into at least three types; the V1a (vascular/hepatic) and V1b (anterior pituitary) receptors which act through phosphatidylinositol hydrolysis to mobilize intracellular Ca2+, and the V2 (kidney) receptor which is coupled to adenylate cyclase. We report here the cloning of a complementary DNA encoding the hepatic V1a arginine vasopressin receptor. The liver cDNA encodes a protein with seven putative transmembrane domains, which binds arginine vasopressin and related compounds with affinities similar to the native rat V1a receptor. The messenger RNA corresponding to the cDNA is distributed in rat tissues known to contain V1a receptors.
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              • Article: not found

              A radioiodinated linear vasopressin antagonist: A ligand with high affinity and specificity for V1areceptors

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                Author and article information

                Journal
                EXN
                Nephron Exp Nephrol
                10.1159/issn.1660-2129
                Cardiorenal Medicine
                S. Karger AG
                1660-2129
                2002
                2002
                30 May 2002
                : 10
                : 3
                : 196-208
                Affiliations
                aUMR CNRS 7519, Université Louis Pasteur, Strasbourg, France; bInstitut d’Anatomie, Université de Zürich, Suisse; cDépartement de Biologie, Faculté des Sciences d’El Jadida, Maroc; dService d’Urologie, Hôpitaux Universitaires de Strasbourg, France
                Article
                58346 Exp Nephrol 2002;10:196–208
                10.1159/000058346
                12053121
                © 2002 S. Karger AG, Basel

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                Page count
                Figures: 6, Tables: 1, References: 49, Pages: 13
                Product
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/58346
                Categories
                Original Paper

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