Chloroquine resistance of Plasmodium berghei: biochemical basis and countermeasures

Bull World Health Organ. 1987;65(3):381-6.

Abstract

Microsomal monooxygenases, enzymes that metabolize xenobiotics, may be responsible for the chloroquine resistance of malarial parasites. Plasmodium cells contain cytochrome P-450 and exhibit aryl hydrocarbon hydroxylase and aminopyrine N-dimethylase activity, two monooxygenases that inactivate chloroquine. The activities of these monooxygenases are considerably higher in chloroquine-resistant strains of Plasmodium berghei than in the chloroquine-sensitive strain of the parasite. Inhibitors of microsomal monooxygenases have the potential to overcome the chloroquine resistance of Plasmodium spp., and, of those inhibitors tested, the copper-lysine complex, copper(lysine)(2), was the most effective.

MeSH terms

  • Aminopyrine N-Demethylase / metabolism*
  • Animals
  • Aryl Hydrocarbon Hydroxylases / metabolism*
  • Chloroquine / pharmacology*
  • Copper / pharmacology*
  • Drug Resistance
  • Enzyme Inhibitors / pharmacology
  • Lysine / analogs & derivatives*
  • Lysine / pharmacology
  • Malaria / blood
  • Malaria / enzymology*
  • Mice
  • Plasmodium berghei / drug effects
  • Plasmodium berghei / enzymology*

Substances

  • Enzyme Inhibitors
  • copper-lysine complex
  • Copper
  • Chloroquine
  • Aryl Hydrocarbon Hydroxylases
  • Aminopyrine N-Demethylase
  • Lysine