G-proteins modulate amiloride-sensitive sodium channels

James K. Bubien, Richard S. Jope, David G. Warnock

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

We examined the regulation of an amiloride-sensitive sodium conductance expressed in human B lymphoid cells. This conductance was activated by two independent pathways, one involving cyclic adenylyl monophosphate (cAMP)- dependent protein kinase and the other involving a pertussis toxin-sensitive G-protein. Cholera toxin, presumably by increasing cellular cAMP, and pertussis toxin, which ADP-ribosylates certain GTP-binding proteins, both independently increased the amiloride-sensitive sodium conductance. Simultaneous treatment with both toxins, however, failed to increase the sodium conductance, implying that a single set of sodium channels was being affected by both toxins. In cells preactivated with pertussis toxin, 8- chlorophenylthio-cAMP inhibited the activated sodium conductance back to the basal level. Thus, cyclic AMP-dependent pathways can either activate or inhibit amiloride-sensitive sodium channels, depending upon the activation state of a pertussis toxin-sensitive GTP-binding protein. These findings support a hypothesis for the regulation of amiloride-sensitive sodium channels which incorporates the independent effects of cholera and pertussis toxins, and in which cyclic AMP can play a dual role in the regulation of channel activity.

Original languageEnglish (US)
Pages (from-to)17780-17783
Number of pages4
JournalJournal of Biological Chemistry
Volume269
Issue number27
StatePublished - Jul 8 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Bubien, J. K., Jope, R. S., & Warnock, D. G. (1994). G-proteins modulate amiloride-sensitive sodium channels. Journal of Biological Chemistry, 269(27), 17780-17783.