4.2 Article

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

Journal

INTEGRATIVE BIOLOGY
Volume 3, Issue 2, Pages 134-141

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c0ib00018c

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Funding

  1. Nano Systems Institute-National Core Research Center (NSI-NCRC)
  2. World Class University (WCU) Program [R31-2008-000-10083-0]
  3. Korea Research Foundation (MOEHRD) [KRF-J03003]
  4. Ministry of Education, Science and Technology, Korea [R01-2007-000-20441-0, 2010-0008225]
  5. Ministry of Health Welfare [A080143]

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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.

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