title: Aquaporin water channels: molecular mechanisms for human diseases.
abstract: Although water is the major component of all biological fluids, the molecular pathways for water transport across cell membranes eluded identification until the discovery of the aquaporin family of water channels. The atomic structure of mammalian AQP1 illustrates how this family of proteins is freely permeated by water but not protons (hydronium ions, H3O+). Definition of the subcellular sites of expression predicted their physiological functions and potential clinical disorders. Analysis of several human disease states has confirmed that aquaporins are involved in multiple different illnesses including abnormalities of kidney function, loss of vision, onset of brain edema, starvation, and arsenic toxicity.
authors: Departments of Biological Chemistry and Medicine, Johns Hopkins School of Medicine, Baltimore, MD 21205-2185, USA. pagre@jhmi.edu
authors: Peter
authors: P
authors: Agre
authors: David
authors: D
authors: Kozono
mesh_terms: D020346:Aquaporins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002386:Cataract / Q000151:congenital / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007668:Kidney / Q000378:metabolism; D007674:Kidney Diseases / Q000235:genetics / Q000378:metabolism; D007908:Lens, Crystalline / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D010802:Phylogeny; D011487:Protein Conformation; D014867:Water / Q000378:metabolism
chemical_list: D020346:Aquaporins; D014867:Water