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Aquaporin water channels – from atomic structure to clinical medicine
Author(s) -
Agre Peter,
King Landon S.,
Yasui Masato,
Guggino Wm B.,
Ottersen Ole Petter,
Fujiyoshi Yoshinori,
Engel Andreas,
Nielsen Søren
Publication year - 2002
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2002.020818
Subject(s) - aquaporin , aquaporin 1 , water channel , tetramer , aquaporin 2 , nephrogenic diabetes insipidus , human physiology , biology , biophysics , microbiology and biotechnology , aquaporin 4 , osmoregulation , chemistry , biochemistry , genetics , kidney , endocrinology , ecology , mechanical engineering , salinity , engineering , inlet , enzyme
The 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.