An extracellular residue determines the agonist specificity of v-2 vasopressin receptors
FEBS letters. Bd. 362. H. 1. Amsterdam: Elsevier 1995 S. 19 - 23
Erscheinungsjahr: 1995
ISBN/ISSN: 0014-5793
Publikationstyp: Zeitschriftenaufsatz
Sprache: Englisch
Doi/URN: 10.1016/0014-5793(95)00150-8
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Inhaltszusammenfassung
The specific V-2 agonist 1-deamino [8-D-arginine]vasopressin (dDAYP), used for treatment of central diabetes insipidus, binds to vasopressin V-2 receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin, In contrast, the V-1 receptors and the porcine V-2 receptor do not tolerate a D-arginine in position 8 of vasopressin, By site directed mutagenesis of the cloned bovine and porcine V-2 receptors we identified a residue (Asp-103) in...The specific V-2 agonist 1-deamino [8-D-arginine]vasopressin (dDAYP), used for treatment of central diabetes insipidus, binds to vasopressin V-2 receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin, In contrast, the V-1 receptors and the porcine V-2 receptor do not tolerate a D-arginine in position 8 of vasopressin, By site directed mutagenesis of the cloned bovine and porcine V-2 receptors we identified a residue (Asp-103) in the first extracellular loop of vasopressin receptors which is responsible for high affinity binding of dDAVP.» weiterlesen» einklappen
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Medizin