Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane

Redox Biol. 2020 Jan:28:101326. doi: 10.1016/j.redox.2019.101326. Epub 2019 Sep 12.

Abstract

Hydrogen peroxide (H2O2) is an essential second intracellular messenger. To reach its targets in the cytosol, H2O2 must cross a membrane, a feat that requires aquaporins (AQP) endowed with 'peroxiporin' activity (AQP3, AQP8, AQP9). Here, we exploit different organelle-targeted H2O2-sensitive probes to show that also AQP11 efficiently conduits H2O2. Unlike other peroxiporins, AQP11 is localized in the endoplasmic reticulum (ER), accumulating partly in mitochondrial-associated ER membranes (MAM). Its downregulation severely perturbs the flux of H2O2 through the ER, but not through the mitochondrial or plasma membranes. These properties make AQP11 a potential regulator of ER redox homeostasis and signaling.

Keywords: Aquaporins; Endoplasmic reticulum; Hydrogen peroxide; Membrane permeability; Peroxiporins; Redox homeostasis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aquaporins / genetics*
  • Aquaporins / metabolism*
  • Biological Transport
  • CHO Cells
  • COS Cells
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Cricetulus
  • Down-Regulation
  • Endoplasmic Reticulum / metabolism*
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Hydrogen Peroxide / pharmacokinetics*

Substances

  • AQP11 protein, human
  • Aquaporins
  • Hydrogen Peroxide