Referenced in: none

Automatically associated channels: Slo1

Title: Fluid-shear-stress-induced translocation of aquaporin-2 and reorganization of actin cytoskeleton in renal tubular epithelial cells.

Authors: Kyung-Jin Jang, Hye Sung Cho, Do Hyun Kang, Won Gyu Bae, Tae-Hwan Kwon, Kahp-Yang Suh

Journal, date & volume: Integr Biol (Camb), 2011 Feb 8 , 3, 134-41

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/21079870

Abstract
In vivo, renal tubular epithelial cells are exposed to luminal fluid shear stress (FSS) and a transepithelial osmotic gradient. In this study, we used a simple collecting-duct-on-a-chip to investigate the role of an altered luminal microenvironment in the translocation of aquaporin-2 (AQP2) and the reorganization of actin cytoskeleton (F-actin) in primary cultured inner medullary collecting duct (IMCD) cells of rat kidney. Immunocytochemistry demonstrated that 3 h of exposure to luminal FSS at 1 dyn cm(-2) was sufficient to induce depolymerization of F-actin in those cells. We observed full actin depolymerization after 5 h exposure and substantial re-polymerization within 2 h of removing the luminal FSS, suggesting that the process is reversible and the fluidic environment regulates the reorganization of intracellular F-actin. We demonstrate that several factors (i.e., luminal FSS, hormonal stimulation, transepithelial osmotic gradient) collectively exert a profound effect on the AQP2 trafficking in the collecting ducts, which is associated with actin cytoskeletal reorganization.