Novel high molecular weight albumin-conjugated angiotensin II activates β-arrestin and G-protein pathways

ARRB2 (β-Arrestin-2) Deficiency Alters Fluid Homeostasis and Blood Pressure Regulation

“…It is notable that the acute injection of these analogs induced excessive saline intake. 35-37 It is possible that the differences between these acute studies and our results in a chronic setting indicate that long-term activation of β-arrestins could induce distinct molecular signals that differ from the short-term effects. Indeed, it was reported that different biased agonists of the AT 1 R mediate subtly different intracellular signals.…”

Insights Into the Role of Angiotensin-II AT 1 Receptor-Dependent β-Arrestin Signaling in Cardiovascular Disease

“…It is notable that other groups have reported that acute activation of β-arrestin using BSA-AngII or SII-Ang II promotes saline intake in rats. 83,84 It remains unclear what causes this discrepancy. Is it a species difference (mouse versus rat)?…”

From Agonist to Antagonist: Modulation of the Physiological Action of Angiotensins by Protein Conjugation—Hemodynamics and Behavior

“…In Torres-Tirado et al (2013 ), the inverse ratio was established between the rate of AT1R internalization and desensitization from molecular mass of polymeric AngII-containing ligands. Based on the assumption that the high molecular weight ligand will be less susceptible to internalization, other authors ( Pang et al, 2019 ) studied the signaling properties of the chemically synthesized AngII-BSA peptide–protein complex, in which 10–12 molecules of AngII are bound to one BSA molecule. Such a ligand was developed as less capable of internalizing agonist supposedly inhibiting the ß-arrestin–biased pathway for signal transduction, which, as is known, is activated with the involvement of internalized AT1 ( Reiter et al, 2017 ).…”