Urea transport mediated by aquaporin water channel proteins

Abstract

Aquaporins (AQPs) are a family of membrane water channels that basically function as regulators of intracellular and intercellular water fow. To date, thirteen aquaporins have been characterized. They are distributed wildly in specifc cell types in multiple organs and tissues. Each AQP channel consists of six membrane-spanning alpha-helices that have a central water-transporting pore. Four AQP monomers assemble to form tetramers, which are the functional units in the membrane. Some of AQPs also transport urea, glycerol, ammonia, hydrogen peroxide, and gas molecules. AQP-mediated osmotic water transport across epithelial plasma membranes facilitates transcellular fuid transport and thus water reabsorption. AQP-mediated urea and glycerol transport is involved in energy metabolism and epidermal hydration. AQP-mediated CO2 and NH3 transport across membrane maintains intracellular acid-base homeostasis. AQPs are also involved in the pathophysiology of a wide range of human diseases (including water disbalance in kidney and brain, neuroin-fammatory disease, obesity, and cancer). Further work is required to determine whether aquaporins are viable therapeutic targets or reliable diagnostic and prognostic biomarkers.