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Aquaporin-8 (AQP8) is an integral membrane protein channel that facilitates the passive transport of water and small uncharged solutes, including hydrogen peroxide and ammonia, across biological membranes in response to osmotic gradients[3]. Found in organs such as the liver, colon, and pancreas, as well as in mitochondria and the endoplasmic reticulum, AQP8 plays crucial roles in maintaining cellular osmotic balance, bile formation, ammonia detoxification, and modulating mitochondrial oxidative stress[2][3]. Its function is regulated by post-translational modifications (e.g., persulfidation at cysteine 53), which can dynamically gate the channel in response to cellular signals and stresses[1]. Dysfunction or altered expression of AQP8 is associated with diseases involving disrupted fluid or ammonia homeostasis and oxidative stress[3].
Inhibitors (e.g., mercury, copper) block channel conductance by interacting with cysteine residues, blocking water and small molecule permeation[2][3].
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