An extracellular residue determines the agonist specificity of V2 vasopressin receptors
- 27 March 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 362 (1) , 19-23
- https://doi.org/10.1016/0014-5793(95)00150-8
Abstract
The specific V2 agonist 1-deamino [8-d-arginine]-vasopressin (dDAVP), used for treatment of central diabetes insipidus, binds to vasopressin V2 receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin. In contrast, the V1 receptors and the porcine V2 receptor do not tolerate a D-arginine in position 8 of vasopressin. By site directed mutagenesis of the cloned bovine and porcine V2 receptors we identified a residue (Asp-103) in the first extracellular loop of vasopressin receptors which is responsible for high affinity binding of dDAVPKeywords
This publication has 21 references indexed in Scilit:
- Hormonal Signaling and Regulation of Salt and Water Transport in the Collecting DuctAnnual Review of Physiology, 1994
- Direct identification of an extracellular agonist binding site in the renal V2 vasopressin receptorBiochemistry, 1993
- Cloning and expression of apical membrane water channel of rat kidney collecting tubuleNature, 1993
- Cloning and characterization of a vasopressin V2 receptor and possible link to nephrogenic diabetes insipidusNature, 1992
- Molecular cloning of the receptor for human antidiuretic hormoneNature, 1992
- Molecular cloning and expression of a rat Via arginine vasopressin receptorNature, 1992
- Radioligand binding studies reveal marked species differences in the vasopressin V1 receptor of rat, rhesus and human tissuesLife Sciences, 1992
- Characterization of specific receptors for vasopressin in the pituitary glandBiochemical and Biophysical Research Communications, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Renal Adenyl Cyclase: Anatomically Separate Sites for Parathyroid Hormone and VasopressinScience, 1968