Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/110177
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dc.contributor.authorKourghi, M.en
dc.contributor.authorNourmohammadi, S.en
dc.contributor.authorPei, J.en
dc.contributor.authorQiu, J.en
dc.contributor.authorMcGaughey, S.en
dc.contributor.authorTyerman, S.en
dc.contributor.authorByrt, C.en
dc.contributor.authorYool, A.en
dc.date.issued2017en
dc.identifier.citationInternational Journal of Molecular Sciences, 2017; 18(11):2323-1-2323-19en
dc.identifier.issn1422-0067en
dc.identifier.issn1422-0067en
dc.identifier.urihttp://hdl.handle.net/2440/110177-
dc.description.abstractAquaporins (AQPs) are known to facilitate water and solute fluxes across barrier membranes. An increasing number of AQPs are being found to serve as ion channels. Ion and water permeability of selected plant and animal AQPs (plant Arabidopsis thaliana AtPIP2;1, AtPIP2;2, AtPIP2;7, human Homo sapiens HsAQP1, rat Rattus norvegicus RnAQP4, RnAQP5, and fly Drosophila melanogaster DmBIB) were expressed in Xenopus oocytes and examined in chelator-buffered salines to evaluate the effects of divalent cations (Ca2+, Mg2+, Ba2+ and Cd2+) on ionic conductances. AtPIP2;1, AtPIP2;2, HsAQP1 and DmBIB expressing oocytes had ionic conductances, and showed differential sensitivity to block by external Ca2+. The order of potency of inhibition by Ca2+ was AtPIP2;2 > AtPIP2;1 > DmBIB > HsAQP1. Blockage of the AQP cation channels by Ba2+ and Cd2+ caused voltage-sensitive outward rectification. The channels with the highest sensitivity to Ca2+ (AtPIP2;1 and AtPIP2;2) showed a distinctive relief of the Ca2+ block by co-application of excess Ba2+, suggesting that divalent ions act at the same site. Recognizing the regulatory role of divalent cations may enable the discovery of other classes of AQP ion channels, and facilitate the development of tools for modulating AQP ion channels. Modulators of AQPs have potential value for diverse applications including improving salinity tolerance in plants, controlling vector-borne diseases, and intervening in serious clinical conditions involving AQPs, such as cancer metastasis, cardiovascular or renal dysfunction.en
dc.description.statementofresponsibilityMohamad Kourghi, Saeed Nourmohammadi, Jinxin V. Pei, Jiaen Qiu, Samantha McGaughey, Stephen D. Tyerman, Caitlin S. Byrt and Andrea J. Yoolen
dc.language.isoenen
dc.publisherMDPIen
dc.rights© 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en
dc.subjectWater channel; aquaporin; Arabidopsis; Drosophila; vertebrates; invertebrates; regulation; divalent cationsen
dc.titleDivalent cations regulate the ion conductance properties of diverse classes of aquaporinsen
dc.typeJournal articleen
dc.identifier.rmid0030077113en
dc.identifier.doi10.3390/ijms18112323en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP160104641en
dc.relation.granthttp://purl.org/au-research/grants/arc/DE150100837en
dc.relation.granthttp://purl.org/au-research/grants/arc/CE140100008en
dc.identifier.pubid386728-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.library.teamDS10en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Molecular and Biomedical Science publications

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