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Merck
  • Correlation between release of reactive oxygen intermediates and inhibition of Toxoplasma multiplication in mouse peritoneal and alveolar macrophages and kidney cells after in vitro incubation with Obioactin, lonomycin A, muramyl dipeptide, lipopolysaccharide or Toxoplasma lysate antigen.

Correlation between release of reactive oxygen intermediates and inhibition of Toxoplasma multiplication in mouse peritoneal and alveolar macrophages and kidney cells after in vitro incubation with Obioactin, lonomycin A, muramyl dipeptide, lipopolysaccharide or Toxoplasma lysate antigen.

Zentralblatt fur Bakteriologie, Mikrobiologie, und Hygiene. Series A, Medical microbiology, infectious diseases, virology, parasitology (1987-05-01)
A Saito, H Sakurai, T Saito, S Taji, T Miyagami, N Suzuki, H M Seitz, H Osaki
RESUMO

The inhibition of Toxoplasma multiplication inside cells does not correlate with an enhanced release of oxygen intermediates except in the case of peritoneal macrophages treated with Obioactin. The inhibition observed in alveolar macrophages treated with Obioactin, in kidney cells treated with Obioactin or lonomycin A and in peritoneal macrophages treated with lonomycin A was not accompanied by an increment of release of oxygen intermediates. Lipopolysaccharide (LPS) and muramyl dipeptide (MDP) enhanced the release of toxic oxygen intermediates in peritoneal macrophages, but did not have any toxoplasmacidal effect. Adenosine triphosphate (ATP) content increased during Obioactin, MDP or Toxoplasma lysate antigen (TLA) treatment. The actual oxygen consumption of the peritoneal macrophages treated with Obioactin increased dose dependently, but that of TLA-, lonomycin A- or MDP-treated cells did not change. These results suggest that the relationship between the intracellular killing of Toxoplasma protozoa and the release of oxygen intermediates differs according to the cells and/or the stimuli, and that the cellular mechanism of Toxoplasma killing in the peritoneal macrophages treated with Obioactin involves an energy-dependent mechanism.