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Title: V1-like [Arg8]vasopressin binding sites occur in rat hepatocyte nuclei.
Austin Authors: Phillips, P A;Hutchins, A M;Burrell, Louise M ;Risvanis, John;Johnston, Colin I
Affiliation: Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Australia
Issue Date: 11-Jul-1994
Publication information: European Journal of Pharmacology; 259(3): 325-9
Abstract: Arginine vasopressin binding site characterisation was performed on purified nuclei and plasma membranes from livers of Sprague-Dawley rats. [125I][d(CH2)5,Sarc7,Arg8]vasopressin, a selective V1 vasopressin receptor antagonist radioligand, bound to the nuclei in a protein concentration and time dependent manner. Scatchard analysis of nuclear binding sites revealed a single binding site with maximal binding site density (Bmax) of 115 +/- 13 fmol/mg protein and affinity (KD) of 5.2 +/- 0.7 nM. Plasma membrane binding demonstrated a Bmax of 529 +/- 25 fmol/mg protein and KD of 1.9 +/- 0.1 nM. The displacement profile for nuclear binding sites using vasopressin analogues was similar to that for plasma membrane binding sites and was typical of a V1 vasopressin receptor type. There was no evidence of V2-like vasopressin receptor binding using [3H]des-Gly-NH9(2)[d(CH2)5,D-Ile2,Ile4,Arg8]vasopressi n, a selective V2 vasopressin receptor radioligand, in the nuclear or membrane fractions. These results suggest the existence of nuclear V1-like vasopressin binding sites.
Gov't Doc #: 7982462
Type: Journal Article
Subjects: Animals
Arginine Vasopressin.analogs & derivatives.pharmacokinetics
Cell Membrane.drug effects.metabolism
Cell Nucleus.drug effects.metabolism
In Vitro Techniques
Liver.drug effects.metabolism
Protein Biosynthesis
Rats, Sprague-Dawley
Receptors, Vasopressin.drug effects.metabolism
Appears in Collections:Journal articles

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