P A Phillips, A M Hutchins, L M Burrell, J Risvanis, C I Johnston
Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Australia.
European journal of pharmacology 1994 Jul 11Arginine 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.
P A Phillips, A M Hutchins, L M Burrell, J Risvanis, C I Johnston. V1-like [Arg8]vasopressin binding sites occur in rat hepatocyte nuclei. European journal of pharmacology. 1994 Jul 11;259(3):325-9
PMID: 7982462
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