Resolution of the insect ouabain paradox

Proc Natl Acad Sci U S A. 2004 Sep 14;101(37):13689-93. doi: 10.1073/pnas.0403087101. Epub 2004 Sep 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport / drug effects
  • Drosophila melanogaster / cytology
  • Drosophila melanogaster / drug effects*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Malpighian Tubules / cytology
  • Malpighian Tubules / drug effects
  • Malpighian Tubules / metabolism
  • Models, Biological*
  • Organic Anion Transporters / genetics
  • Organic Anion Transporters / metabolism*
  • Ouabain / metabolism
  • Ouabain / pharmacokinetics
  • Ouabain / pharmacology*
  • Phylogeny
  • RNA Interference
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Organic Anion Transporters
  • Ouabain
  • Sodium-Potassium-Exchanging ATPase