Abstract
Aquaporins (AQPs) are proteinaceous channels widespread in nature where they allow facilitated permeation of water and uncharged through cellular membranes. AQPs play a number of important roles in both health and disease. This review focuses on the most recent advances and research trends regarding the expression and modulation, as well as physiological and pathophysiological functions of AQPs in hepatocytes and Sertoli cells (SCs). Besides their involvement in bile formation, hepatocyte AQPs are involved in maintaining energy balance acting in hepatic gluconeogenesis and lipid metabolism, and in critical processes such as ammonia detoxification and mitochondrial output of hydrogen peroxide. Roles are played in clinical disorders including fatty liver disease, diabetes, obesity, cholestasis, hepatic cirrhosis and hepatocarcinoma. In the seminiferous tubules, particularly in SCs, AQPs are also widely expressed and seem to be implicated in the various stages of spermatogenesis. Like in hepatocytes, AQPs may be involved in maintaining energy homeostasis in these cells and have a major role in the metabolic cooperation established in the testicular tissue. Altogether, this information represents the mainstay of current and future investigation in an expanding field.
Highlights
Aquaporins (AQPs) represent channel proteins permeating water, small solutes and certain gases across biological membranes [1]
Based on their biophysical properties of transport and phylogenesis, mammalian AQPs are grouped into orthodox aquaporins, AQPs primarily permeable to water (AQP0, AQP1, AQP2, AQP4, AQP5, AQP6 and Aquaporin 8 (AQP8)) and aquaglyceroporins, AQPs transporting a series of small uncharged solutes, glycerol, in addition to water (AQP3, AQP7, Aquaporin 9 (AQP9), AQP10)
Hepatocyte AQP8 in its N-glycosylated form is found in canalicular membranes and pericanalicular vesicles [6,7,8], while as a non-glycosylated protein is present in inner mitochondrial membranes [9,10]
Summary
Aquaporins (AQPs) represent channel proteins permeating water, small solutes and certain gases across biological membranes [1]. The 2003 Nobel Prize for Chemistry was awarded to Peter Agre for the discovery and functional demonstration [2] of the AQP family of membrane channels (for a letter about Peter Agre, see [3]). Based on their biophysical properties of transport and phylogenesis, mammalian AQPs are grouped into orthodox aquaporins, AQPs primarily permeable to water (AQP0, AQP1, AQP2, AQP4, AQP5, AQP6 and AQP8) and aquaglyceroporins, AQPs transporting a series of small uncharged solutes, glycerol, in addition to water (AQP3, AQP7, AQP9, AQP10). We attempt an overview comprising the most recent advances and research trends on the regulation and function of AQPs in two critically important cell types, namely hepatocytes and Sertoli cells, both in health and disease
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