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- W2012693304 abstract "Recent studies have characterized a specific binding site for the C-terminal 3-8 fragment of angiotensin II (Ang IV). In the present study we looked at the internalization process of this receptor on bovine aortic endothelial cells (BAEC). Under normal culture conditions, BAEC efficiently internalized 125I-Ang IV as assessed by acid-resistant binding. Internalization of 125I-Ang IV was considerably decreased after pretreatment of cells with hyperosmolar sucrose or after pretreatment of BAEC with inhibitors of endosomal acidification such as monensin or NH4Cl. About 50% of internalized 125I-Ang IV recycled back to the extracellular medium during a 2 h incubation at 37°C. 125I-Ang IV remained mostly intact during the whole process of internalization and recycling as assessed by thin layer chromatography. As expected, internalization of 125I-Ang IV was completely abolished by divalinal-Ang IV, a known AT4 receptor antagonist. Interestingly, 125I-divalinal-Ang IV did not internalize into BAEC. These results suggest that AT4 receptor undergoes an agonist-dependent internalization and recycling process commonly observed upon activation of functional receptors. J. Cell. Biochem. 75:587–597, 1999. © 1999 Wiley-Liss, Inc." @default.
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- W2012693304 date "1999-12-15" @default.
- W2012693304 modified "2023-10-11" @default.
- W2012693304 title "Agonist-dependent AT4 receptor internalization in bovine aortic endothelial cells" @default.
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- W2012693304 doi "https://doi.org/10.1002/(sici)1097-4644(19991215)75:4<587::aid-jcb5>3.0.co;2-q" @default.
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