Aquaporin Water Channels--from Atomic Structure to Clinical Medicine

Overview

Journal J Physiol

Specialty Physiology

Date 2002 Jul 4

PMID 12096044

Citations 314

Authors

Peter Agre

Landon S King

Masato Yasui

Wm B Guggino

Ole Petter Ottersen

Yoshinori Fujiyoshi

Andreas Engel

Soren Nielsen

Affiliations

Soon will be listed here.

Abstract

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.

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