PMID: 2499767Jun 1, 1989Paper

Divalent cation-induced interconversion of hepatic angiotensin receptor subtypes

Molecular Pharmacology
J McQueen, P F Semple

Abstract

The effects of divalent cations on the hepatic angiotensin receptor have been investigated using radioligand binding methods. With a plasma membrane-enriched fraction from rat liver, a total binding capacity for angiotensin peptides of 0.5 pmol/mg of membrane protein was observed. In the absence of divalent cations, almost all of these sites showed low affinity (KD, 11.25 nM) for angiotensin II. In the presence of Ca2+, there was a concentration-dependent increase in the proportion of sites with high affinity (KD, 0.94 nM) for angiotensin II. Mg2+, Sr2+, and Ba2+ were less effective in this respect, although Mg2+ also modified affinity of the high affinity subtype. Monovalent cations (Na+, Cs+, and K+) had little effect on angiotensin binding. Both receptor subtypes showed high and approximately equal affinity for sarcosine1-analogues of angiotensin II and 10-fold lower and equal affinity or Ile7-angiotensin III. The low affinity subtype appeared to be more sensitive to N-terminal deletions in the peptide. Interconversion of receptor subtypes could be prevented by 5'-guanylylimidodiphosphate, La3+, diltiazem, and verapamil. The results show that the hepatic angiotensin receptor can exist in high and low affinity states in vitro...Continue Reading

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