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In guinea pig hepatocytes angiotensin II induced phosphorylase a activation. This effect was mimicked by other angiotensins with the potency order: angiotensin II (EC₅₀ 1 nm)>angiotensin III (EC₅₀ 30 nm)>angiotensin I (EC₅₀ 300 nm). The effect of 10 nm angiotensin II was blocked by the angiotensin II receptor AT₁-selective antagonists irbesartan and losartan (K_i values of 1 nm and 10 nm for irbesartan and losartan respectively) but not by the AT₂-selective antagonist PD123177.

Similar data were obtained when the production of [³H]IP₃ from [³H]myo-inositol-labeled cells was studied. Angiotensin II induced a dose-dependent increase in [³H]IP₃ production; the maximal effect (3-fold) was observed at a concentration of 10 µm. This effect of angiotensin II was completely blocked by the AT₁-selective antagonists irbesartan and losartan, but only in a very limited fashion by PD123177. [¹²⁵I][Sar¹-Ile⁸]angiotensin II bound with high affinity (3·8 nm) to a moderately abundant number of sites (660 fmol/mg protein) in guinea pig liver membranes. Binding competition experiments indicate the following orders of potency for agonists: angiotensin II (1·5 nm)>angiotensin III (7 nm)>angiotensin I (176 nm), and for antagonists: irbesartan (0·5 nm)>losartan (36 nm)>> PD123177 (>> 10 000 nm).

The functional and binding data strongly indicate that the effects of angiotensin II were mediated through AT₁ receptors. Expression of the mRNA for these receptors was confirmed by RT-PCR and hybridization of the reaction product with a radiolabeled rat AT₁ receptor cDNA probe.

Journal of Endocrinology (1997) 154, 133–138

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