Influence of superoxide dismutase and catalase on the stimulation by phagocytosis of L-thyroxine and L-triiodothyronine deiodination in the human leukocyte.
Neither superoxide dismutase, which destroys the superoxide radical by catalyzing its conversion to hydrogen peroxide, nor catalase prevented the stimulation by phagocytosis of the deiodination of L-thyroxine or L-triiodothyronine in human leukocytes. On the other hand, superoxide dismutase led to an increase in the proportion of iodinated material, which remained at the origin during chromatography in a butanol-acetic acid-water solvent system, whereas catalase had the opposite effect. The data suggest that neither the superoxide radical nor hydrogen peroxide plays a major role in the stimulation of deiodination of hormone, but that once deiodination has occurred, hydrogen peroxide is more important than that superoxide radical in subsequent iodination reactions within the leukocyte.
D002374:Catalase / Q000494:pharmacology*; D006801:Humans; D007962:Leukocytes / Q000187:drug effects / Q000378:metabolism*; D010587:Phagocytosis / Q000187:drug effects*; D013482:Superoxide Dismutase / Q000494:pharmacology*; D013974:Thyroxine / Q000097:blood*; D014284:Triiodothyronine / Q000097:blood*; D015054:Zymosan / Q000494:pharmacology
D014284:Triiodothyronine; D015054:Zymosan; D002374:Catalase; D013482:Superoxide Dismutase; D013974:Thyroxine