V1-like [Arg8]vasopressin binding sites occur in rat hepatocyte nuclei

Paddy A. Phillips, Anne Marie Hutchins, Louise M. Burrell, John Risvanis, Colin I. Johnston

Research output: Contribution to journalArticlepeer-review


Arginine vasopressin binding site characterization 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-NH29[d(CH2)5,D-Ile2,Ile4,Arg8]vasopressin, a selective V2 vasopressin receptor radioligand, in the nuclear or membrane fractions. These results suggest the existence of nuclear V1-like vasopressin binding sites.

Original languageEnglish
Pages (from-to)325-329
Number of pages5
JournalEuropean Journal of Pharmacology
Issue number3
Publication statusPublished - 11 Jul 1994
Externally publishedYes


  • Cell nucleus
  • Peptide
  • Vasopressin
  • Vasopressin receptor
  • Vasopressin receptor antagonist


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