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Aquaporin water channels--from atomic structure to clinical medicine Agre P; King LS; Yasui M; Guggino WB; Ottersen OP; Fujiyoshi Y; Engel A; Nielsen SJ Physiol 2002[Jul]; 542 (Pt 1): 3-16The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression coincide closely with the clinical phenotypes--ranging from congenital cataracts to nephrogenic diabetes insipidus. More than 200 members of the aquaporin family have been found in plants, microbials, invertebrates and vertebrates, and their importance to the physiology of these organisms is being uncovered.|Animals[MESH]|Aquaporins/chemistry/drug effects/genetics/*metabolism[MESH]|Humans[MESH]|Protein Conformation[MESH]|Tissue Distribution[MESH]|Water/*metabolism[MESH] |
