Subcellular localization and internalization of the vasopressin V1B receptor

European Journal of Pharmacology
Aki KashiwazakiTaka-Aki Koshimizu

Abstract

Only limited information is available on agonist-dependent changes in the subcellular localization of vasopressin V1B receptors. Our radioligand binding study of membrane preparations and intact cells revealed that a large fraction of the V1B receptor is located in the cytoplasm in unstimulated CHO cells, which is in contrast to the plasma membrane localization of the V1A and V2 receptors. Moreover, when the affinity of radiolabeled arginine-vasopressin ([3H]AVP) was compared between membrane preparations and intact cells, the affinity of [3H]AVP to the cell surface V1B receptors, but not the V1A receptors, was significantly reduced. Although the number and affinity of cell surface V1B receptors decreased, they became extensively internalized upon binding with [3H]AVP. Approximately 87% of cell surface-bound [3H]AVP was internalized and became resistant to acid wash during incubation with 1 nM [3H]AVP. By contrast, less ligand (35%) was internalized in the cells expressing the V1A receptor. Extensive internalization of the V1B receptors was partially attenuated by inhibitors of cytoskeletal proteins, siRNA against β-arrestin 2, or the removal of sodium chloride from the extracellular buffer, indicating that this internalization...Continue Reading

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Citations

May 4, 2016·Scientific Reports·Taka-Aki KoshimizuJunichi Taniguchi
Sep 18, 2018·Genes, Brain, and Behavior·Doris S Bayerl, Oliver J Bosch
May 18, 2019·Journal of the American Society of Nephrology : JASN·Torsten GieseckeKerim Mutig
May 18, 2020·Hypertension Research : Official Journal of the Japanese Society of Hypertension·Bojana SavićNina Japundžić-Žigon
Jan 23, 2021·Biomedicines·Samantha SparapaniChiara Gamberi
Aug 6, 2021·Scientific Reports·Nuttawadee NgamlertwongTaka-Aki Koshimizu

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