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.

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

THE neurohypophyseal hormone arginine vasopressin has diverse actions1–7 , 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 types8; the Via (vascular/hepatic)1,9–11and Vlb (anterior pituitary)12 receptors which act through phosphatidylinositol hydrolysis to mobilize intracellular Ca2+, and the V2 (kidney) receptor1,13,14which is coupled to adenylate cyclase. We report here the cloning of a complementary DNA encoding the hepatic Via 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 Via receptor. The messenger RNA corresponding to the cDNA is distributed in rat tissues known to contain Via receptors.

Molecular cloning and expression of a rat V1a arginine vasopressin receptor.

Relationship between inositol polyphosphate production and the increase of cytosolic free Ca2+ induced by vasopressin in isolated hepatocytes.

The neurohypophysial hormone arginine vasopressin (AVP) is essential for a wide range of physiological functions, including water reabsorption, cardiovascular homeostasis, hormone secretion, and social behavior. These and other actions of AVP are mediated by at least three distinct receptor subtypes: V1a, V1b, and V2. Although the antidiuretic action of AVP and V2 receptor in renal distal tubules and collecting ducts is relatively well understood, recent years have seen an increasing understanding of the physiological roles of V1a and V1b receptors. The V1a receptor is originally found in the vascular smooth muscle and the V1b receptor in the anterior pituitary. Deletion of V1a or V1b receptor genes in mice revealed that the contributions of these receptors extend far beyond cardiovascular or hormone-secreting functions. Together with extensively developed pharmacological tools, genetically altered rodent models have advanced the understanding of a variety of AVP systems. Our report reviews the findings in this important field by covering a wide range of research, from the molecular physiology of V1a and V1b receptors to studies on whole animals, including gene knockout/knockdown studies.

Vasopressin V1a and V1b Receptors: From Molecules to Physiological Systems

Role of phosphatidylinositol turnover in alpha1 and of adenylate cyclase inhibition in alpha2 effects of catecholamines

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2877%2981020-X

Rapid stimulation, by vasopressin and adrenaline, of inorganic phosphate incorporation into phosphatidyl inositol in isolated hepatocytes.

The influence of extracellular calcium concentration on the vasopressin-stimulated incorporation of inorganic phosphate into phosphatidylinositol in hepatocyte suspensions.

Terence R. Verrinder

Papers

Rapid stimulation, by vasopressin and adrenaline, of inorganic phosphate incorporation into phosphatidyl inositol in isolated hepatocytes.

The influence of extracellular calcium concentration on the vasopressin-stimulated incorporation of inorganic phosphate into phosphatidylinositol in hepatocyte suspensions.