Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins

The discovery of the water channel aquaporin has greatly expanded our understanding of the regulation of the water permeability of biological membranes. The atomic structure of aquaporin-1 (AQP1) demonstrated how aquaporin is freely permeated by water but not protons and provided marked insight into...

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Main Author: Masato Yasui
Format: Article
Language:English
Published: Elsevier 2004-01-01
Series:Journal of Pharmacological Sciences
Online Access:http://www.sciencedirect.com/science/article/pii/S1347861319323369
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author Masato Yasui
author_facet Masato Yasui
author_sort Masato Yasui
collection DOAJ
description The discovery of the water channel aquaporin has greatly expanded our understanding of the regulation of the water permeability of biological membranes. The atomic structure of aquaporin-1 (AQP1) demonstrated how aquaporin is freely permeated by water but not protons and provided marked insight into several human disorders. Eleven mammalian aquaporins have been identified, each with a distinct distribution, and these are selectively permeated by water or water plus glycerol. Aquaporins are suspected in numerous pathological conditions involving fluid transport such as brain edema. Knowledge of aquaporin structure may provide insight into the development of new therapeutics through appropriate drug design. Keywords:: aquaporin-1, permeability, water channel, structure and function, human disease
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spelling doaj.art-a473c1c45bf842598f4da561c5e147f42022-12-21T17:16:51ZengElsevierJournal of Pharmacological Sciences1347-86132004-01-01963260263Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of AquaporinsMasato Yasui0Departments of Pediatrics and Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA; Corresponding author. E-mail: myasui@jhmi.eduThe discovery of the water channel aquaporin has greatly expanded our understanding of the regulation of the water permeability of biological membranes. The atomic structure of aquaporin-1 (AQP1) demonstrated how aquaporin is freely permeated by water but not protons and provided marked insight into several human disorders. Eleven mammalian aquaporins have been identified, each with a distinct distribution, and these are selectively permeated by water or water plus glycerol. Aquaporins are suspected in numerous pathological conditions involving fluid transport such as brain edema. Knowledge of aquaporin structure may provide insight into the development of new therapeutics through appropriate drug design. Keywords:: aquaporin-1, permeability, water channel, structure and function, human diseasehttp://www.sciencedirect.com/science/article/pii/S1347861319323369
spellingShingle Masato Yasui
Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
Journal of Pharmacological Sciences
title Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
title_full Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
title_fullStr Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
title_full_unstemmed Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
title_short Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Structure and Function of Aquaporins
title_sort molecular mechanisms and drug development in aquaporin water channel diseases structure and function of aquaporins
url http://www.sciencedirect.com/science/article/pii/S1347861319323369
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