Myeloperoxidase is more efficient than eosinophil peroxidase in the in vitro killing of newborn larvae of Trichinella spiralis.
Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) catalyse the formation of hypochlorite (OCl-) from chloride ions (OCl-) and hydrogen peroxide (H2O2). OCl- proved to be highly toxic for Trichinella spiralis newborn larvae (NBL) in in vitro assays. Using purified human MPO and EPO it was found that even at neutral pH both enzymes under appropriate conditions are able to kill NBL. The rate at which OCl- is produced is much lower in the EPO- than in the MPO-mediated reaction. This difference in enzymic activity may explain why in the MPO-mediated reaction half the amount of OCl- was sufficient to kill 50% of the NBL, as compared to the EPO-mediated reaction. Purified human eosinophil major basic protein showed excellent OCl- scavenging properties, resulting in a significant decrease in the EPO-mediated NBL killing. Addition of ammonium ions [(NH4)2SO4] to the EPO-mediated reaction increased the NBL killing remarkably. It was concluded that in vitro MPO is more efficient than EPO in killing NBL. Furthermore, it was suggested that although eosinophils show marked parasiticidal effects in various in vitro systems, their primary biological role might be the regulation of the inflammatory reactions.
D000818:Animals; D000969:Antinematodal Agents; D047209:Eosinophil Peroxidase; D006997:Hypochlorous Acid / Q000378:metabolism; D007814:Larva / Q000187:drug effects; D009195:Peroxidase / Q000494:pharmacology*; D010544:Peroxidases / Q000494:pharmacology*; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D014234:Trichinella / Q000187:drug effects*
D000969:Antinematodal Agents; D000644:Quaternary Ammonium Compounds; D006997:Hypochlorous Acid; D047209:Eosinophil Peroxidase; D010544:Peroxidases; D009195:Peroxidase