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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Format: | Article |
Language: | English |
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Elsevier
2004-01-01
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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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format | Article |
id | doaj.art-a473c1c45bf842598f4da561c5e147f4 |
institution | Directory Open Access Journal |
issn | 1347-8613 |
language | English |
last_indexed | 2024-12-24T03:42:17Z |
publishDate | 2004-01-01 |
publisher | Elsevier |
record_format | Article |
series | Journal of Pharmacological Sciences |
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 |
work_keys_str_mv | AT masatoyasui molecularmechanismsanddrugdevelopmentinaquaporinwaterchanneldiseasesstructureandfunctionofaquaporins |