Peptidic ligands induce significant internalization of AT1 receptors, whereas the non-peptidic antagonist DuP753 is far less potent, and receptor activation/G-protein coupling are not required.
Receptor activation and G-protein coupling are not required for AT1a internalization, and peptidic ligands are more potent at inducing internalization than non-peptidic antagonists.
The capacity of the angiotensin II (AngII) agonist Sar1AngII, the antagonist Sar1-Ile8AngII and the non-peptidic antagonist DuP753 to undergo receptor internalization were studied in Chinese hamster ovary cells expressing rat AngII type 1a or 1b receptors (AT1a or AT1b) or a mutant of AT1a (Asn74) unable to couple G-protein. In this expression system, the ligand-induced internalization of rat AT1a and AT1b are similar. Moreover, peptidic ligands, either the agonist or antagonist, induce a significant internalization of AT1 receptors, but the non-peptidic antagonist DuP753 is far less potent. Finally, the normal internalization of the mutant Asn74 demonstrates that receptor activation and G-protein coupling are not required for AT1a internalization.
Conchon et al. (Mon,) reported a other. [Sar1]AngII, [Sar1-Ile8]AngII, and DuP753 was evaluated on Receptor internalization. Peptidic ligands induce significant internalization of AT1 receptors, whereas the non-peptidic antagonist DuP753 is far less potent, and receptor activation/G-protein coupling are not required.
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