The discovery of water channels (aquaporins) was a breakthrough in research on water transport. Aquaporins are a family of intrinsic membrane proteins that function as water, selective channels (except aquaporin-3 and aquaporin-7, which are permeable to urea and glycerol as well) in the plasma membranes of many cells. Aquaporin-0 (MIP26) functions to maintain fluid balance in the lens. Aquaporin-1 is involved in water reabsorption in the kidney's proximal tubules and the thin descending Henle's loop, aqueous humor formation in eye, cerebrospinal fluid formation in brain, and airway hydration in lung. Aquaporin-2 is the only water channel that is activated by vasopressin to enhance water reabsorption in the kidney collecting duct. Aquaporin-3 also contributes to water reabsorption in the kidney collecting duct but is unresponsive to vasopressin. It also appears that aquaporin-3 may contribute to cornea transparency. Aquaporin-4 is involved in cerebrospinal fluid transport in brain, water transport in the kidney collecting duct, aqueous humor transport in the eye, and airway hydration in the lung. Aquaporin-5 apparently is coupled to fluid secretion in exocrine tissues. Although the exact function of aquaporin-6 is not known due to its uncertain localization, its restricted presence in the kidney may suggest a potential role in water transport. Aquaporin-7 appears to play a role in the cryopreservation of the sperm whereas aquaporin-8 is responsible for the secretion of pancreatic juice. The major focus of this review is a discussion of aquaporins in renal epithelia, and particularly the mechanisms associated with vasopressin, mediated water transport involving aquaporin-2 and the signal transduction pathways linked to vasopressin action.
|Number of pages||17|
|Journal||Proceedings of the Society for Experimental Biology and Medicine|
|State||Published - Dec 1998|