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Citation
Torrie, L.S., Radford, J.C., Southall, T.D., Kean, L., Dinsmore, A.J., Davies, S.A., Dow, J.A. (2004). Resolution of the insect ouabain paradox.  Proc. Natl. Acad. Sci. U.S.A. 101(37): 13689--13693.
FlyBase ID
FBrf0180636
Publication Type
Research paper
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.

PubMed ID
PubMed Central ID
PMC518814 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Proc. Natl. Acad. Sci. U.S.A.
    Title
    Proceedings of the National Academy of Sciences of the United States of America
    Publication Year
    1915-
    ISBN/ISSN
    0027-8424
    Data From Reference
    Alleles (4)
    Gene Groups (1)
    Genes (11)
    Insertions (2)
    Experimental Tools (1)
    Transgenic Constructs (1)