Modulation of macrophage interaction with Trypanosoma cruzi by phospholipase A2-sensitive components of the parasite membrane.
The presence of phospholipase A2 (PLA2) significantly increased the association between Trypanosoma cruzi and macrophages. This effect reflected alterations to the parasite membrane since it was reproduced only when the parasite but not the macrophage was pretreated with PLA2. That PLA2 activity was responsible for the noted enhancement was indicated by the ability of the specific substrate phosphatidylcholine to block it. The presence of the PLA2 inhibitors quinacrine, 4-bromophenacyl bromide or phentermine markedly inhibited parasite-macrophage association. Quinacrine also inhibited association of the parasite with a non-phagocytic host cell. These results suggested a role for endogenous PLA2 in the initial stages of cell infection by T. cruzi.
D000818:Animals; D002478:Cells, Cultured; D006790:Host-Parasite Interactions; D008264:Macrophages / Q000469:parasitology*; D051379:Mice; D008815:Mice, Inbred Strains; D010713:Phosphatidylcholines / Q000494:pharmacology; D010740:Phospholipases / Q000494:pharmacology*; D010741:Phospholipases A / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D054467:Phospholipases A2; D014349:Trypanosoma cruzi / Q000187:drug effects* / Q000201:enzymology / Q000502:physiology
D010713:Phosphatidylcholines; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2