Chloroquine inhibition of cholera toxin

Yi fan Liang, Johnny W. Peterson, Christopher A. Jackson, James C. Reitmeyer

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Cholera toxin (CT) stimulated adenylate cyclase and a phospholipase which elevated levels of 3.5-cyclic adenosine monophosphate (cAMP) and arachidonic acid (AA). The AA was quickly converted to prostaglandins (PGs) via the cyclo-oxygenase pathway. Chloroquine exerted minimal inhibition of cAMP levels in CT-treated cells, although CT-induced release of [3H]AA and PGs was blocked completely when the drug was added in concentrations as low as 0.1 mM (30 μγ ml). Inhibition of [3H]AA release was complete when chloroquine was added before or within 30 min after CT. The capacity of chloroquine to inhibit either phospholipase C (PLC) or phospholipase A2 (PLA2) could explain the antisecretory activity of this drug.

Original languageEnglish (US)
Pages (from-to)143-145
Number of pages3
JournalFEBS Letters
Volume275
Issue number1-2
DOIs
StatePublished - Nov 26 1990

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Liang, Y. F., Peterson, J. W., Jackson, C. A., & Reitmeyer, J. C. (1990). Chloroquine inhibition of cholera toxin. FEBS Letters, 275(1-2), 143-145. https://doi.org/10.1016/0014-5793(90)81459-2