Peter Agre (2014) - Aquaporin Water Channels – From Atomic Structure to Malaria

Peter Agre (2014)

Aquaporin Water Channels – From Atomic Structure to Malaria

Peter Agre (2014)

Aquaporin Water Channels – From Atomic Structure to Malaria

Abstract

Aquaporin (AQP) water channel proteins enable high water permeability in certain biological membranes. Discovered in human red cells but expressed in multiple tissues, AQP1 has been thoroughly characterized and its atomic structure is known. Expression patterns of the 13 known human homologs predict phenotype. Individuals lacking Colton blood group antigens have mutations in AQP1. In people with no AQP1, lack of water causes defective urine concentration and reduced fluid exchange between capillary and interstitium in lung. Mutations in AQP0, expressed in lens fiber cells, result in familial cataracts. Mutations in AQP2, expressed in renal collecting duct principal cells, result in severe nephrogenic diabetes insipidus. AQP2 underexpression is found in disorders with reduced urinary concentration, AQP2 overexpression in those with fluid retention.
Mistargeting of AQP5, normally expressed in the apical membranes of salivary and lacrimal gland acini, can occur in Sjogren’s syndrome. Aquaporins also are implicated in brain edema and muscular dystrophy (AQP4), anhidrosis (AQP5), renal tubular acidosis (AQP6), conversion of glycerol to glucose during starvation (AQP7 and AQP9) and cystic fibrosis (several aquaporins). Aquaporins provide rootlet water uptake and turgor in plants. Recent work has delineated roles for aquaporins in parasitic diseases including malaria.

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