Aquaporin water channels - From atomic structure to clinical medicine

Peter Agre, Landon S. King, Masato Yasui, Wm B. Guggino, Ole Petter Ottersen, Yoshinori Fujiyoshi, Andreas Engel, Søren Nielsen

Research output: Contribution to journalReview article

802 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3-16
Number of pages14
JournalJournal of Physiology
Volume542
Issue number1
DOIs
Publication statusPublished - 2002 Jul 1
Externally publishedYes

ASJC Scopus subject areas

  • Physiology

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    Agre, P., King, L. S., Yasui, M., Guggino, W. B., Ottersen, O. P., Fujiyoshi, Y., Engel, A., & Nielsen, S. (2002). Aquaporin water channels - From atomic structure to clinical medicine. Journal of Physiology, 542(1), 3-16. https://doi.org/10.1113/jphysiol.2002.020818