Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/73722
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dc.contributor.authorYool, A.en
dc.contributor.authorCampbell, E.en
dc.date.issued2012en
dc.identifier.citationMolecular Aspects of Medicine, 2012; 33(5-6):553-561en
dc.identifier.issn0098-2997en
dc.identifier.issn1872-9452en
dc.identifier.urihttp://hdl.handle.net/2440/73722-
dc.description.abstractAquaporins have been assumed to be selective for water alone, and aquaglyceroporins are accepted as carrying water and small uncharged solutes including glycerol. This review presents an expanded view of aquaporins as channels with more complex mechanisms of regulation and diverse repertoires of substrate permeabilities than were originally appreciated in the early establishment of the field. The role of aquaporins as dual water and gated ion channels is likely to have physiological and potentially translational relevance, and can be evaluated with newly developed molecular and pharmacological tools. Ion channel activity has been shown for Aquaporins -0, -1, and -6, Drosphila Big Brain, and plant Nodulin-26. Although the concept of ion channel function in aquaporins remains controversial, research advances are beginning to define not only the ion channel function but also the detailed molecular mechanisms that govern and mediate the multifunctional capabilities. With regard to physiological relevance, the adaptive benefit of expression of ion channel activity in aquaporins, implied by amino acid sequence conservation of the ion channel gating domains, suggests they provide more than water or glycerol and solute transport. Dual ion and water channels are of interest for understanding the modulation of transmembrane fluid gradients, volume regulation, and possible signal transduction in tissues expressing classes of aquaporins that have the dual function capability. Other aquaporin classes might be found in future work to have ion channel activities, pending identification of the possible signaling pathways that could govern activation.en
dc.description.statementofresponsibilityAndrea J. Yool, Ewan M. Campbellen
dc.language.isoenen
dc.publisherPergamonen
dc.rightsCopyright © 2012 Elsevier Ltd. All rights reserved.en
dc.subjectMIP; Arylsulfonamide; Nonselective cation channel; Cyclic GMP; AQP; Fluid transporten
dc.titleStructure, function and translational relevance of aquaporin dual water and ion channelsen
dc.typeJournal articleen
dc.identifier.rmid0020121840en
dc.identifier.doi10.1016/j.mam.2012.02.001en
dc.identifier.pubid23244-
pubs.library.collectionPhysiology publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidYool, A. [0000-0003-1283-585X]en
Appears in Collections:Physiology publications

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