Selenium metabolism and glutathione peroxidase activity in cultured human lymphoblasts. Effects of transsulfuration defects and pyridoxal phosphate.
The metabolism of selenite, selenocysteine (SeCys), and selenomethionine (SeMet) was studied in three human lymphoblast cell lines with defects in the transsulfuration pathway and in control cells without this defect. There were very little differences in the induction of glutathione peroxidase (GPX) activity by selenite and SeCys among these cells. However, markedly higher levels of SeMet were required to induce GPX activity in transsulfuration defective cells than in control cells. Surprisingly, the addition of pyridoxal phosphate (PLP) to the media resulted in elevated GPX activity in all cells regardless of the chemical form of Se used. There is no explanation for this effect of PLP, but it is not through direct reaction with GPX or on the alteration of sulfhydryl groups.
D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D004790:Enzyme Induction; D005979:Glutathione Peroxidase / Q000378:metabolism*; D006801:Humans; D008214:Lymphocytes / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D009154:Mutation; D011732:Pyridoxal Phosphate / Q000494:pharmacology*; D012643:Selenium / Q000378:metabolism*; D017279:Selenocysteine / Q000378:metabolism / Q000494:pharmacology; D012645:Selenomethionine / Q000378:metabolism / Q000494:pharmacology
D017279:Selenocysteine; D011732:Pyridoxal Phosphate; D012645:Selenomethionine; D005979:Glutathione Peroxidase; D012643:Selenium