Resolution of the insect ouabain paradox

Torrie, L., Radford, J., Southall, T., Kean, L., Dinsmore, A., Davies, S. and Dow, J. (2004) Resolution of the insect ouabain paradox. Proceedings of the National Academy of Sciences of the United States of America, 101(37), pp. 13689-13693. (doi: 10.1073/pnas.0403087101) (PMID:15347816) (PMCID:PMC518814)

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Abstract

Many insects are highly resistant to plant toxins, such as the cardiac glycoside ouabain. How can the epithelia that must handle such toxins, also be refractory to them? In Drosophila, the Malpighian (renal) tubule contains large amounts of Na+,K+ ATPase that is known biochemically to be exquisitely sensitive to ouabain, yet the intact tissue is almost unaffected by even extraordinary concentrations. The explanation is that the tubules are protected by an active ouabain transport system, colocated with the Na+,K+ ATPase, thus preventing ouabain from reaching inhibitory concentrations within the basolateral infoldings of principal cells. These data show that the Na+,K+ ATPase, previously thought to be unimportant, may be as vital in insect tissues as in vertebrates, but can be cryptic to conventional pharmacology.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Dow, Professor Julian and Davies, Professor Shireen
Authors: Torrie, L., Radford, J., Southall, T., Kean, L., Dinsmore, A., Davies, S., and Dow, J.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Proceedings of the National Academy of Sciences of the United States of America
Publisher:National Academy of Sciences
ISSN:0027-8424
ISSN (Online):1091-6490

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
343251Comparative integrative physiology of novel branches of the NA+/H+ exchanger familyJulian DowBiotechnology and Biological Sciences Research Council (BBSRC)S19561Institute of Molecular Cell and Systems Biology