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- W102512913 abstract "B-lymphocytes, monocytes, and partially differentiated human leukemic cell lines express 5-lipoxygenase protein but no concomitant cellular activity. Recently, we and others could show that glutathione peroxidases (GPx) are responsible for inhibition of 5-lipoxygenase activity in these cell lines [1,2]. Characterization of the endogenous 5-lipoxygenase inhibitors in the B-lymphocytic cell line BL41-E95A and in HL-60 cells demonstrated that the respective inhibitors display properties identical to GPx-4 [2]. Characterization of the functionality of this inhibitor revealed that inhibition of 5-lipoxygenase in these cell lines was abolished when 5-LO activity was determined in cell homogenates in the absence of thiols. In contrast to these findings, monocytic cells contain an endogenous inhibitor which suppresses 5-lipoxygenase activity in intact cells and in cell homogenates both in the presence and absence of thiols (Figure 1). Purification of this endogenous 5-LO inhibitor of monocytic cells followed by protein sequencing and immunoblotting revealed that the inhibitor is GPx-1. In contrast to peroxidase activity, there was no requirement for millimolar concentrations of thiols for 5-LO inhibition indicating that different catalytic properties of peroxidases are addressed by these two actions.KeywordsGlutathione PeroxidaseMyeloid CellCell HomogenateMonocytic CellHuman Leukemic Cell LineThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
- W102512913 created "2016-06-24" @default.
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- W102512913 date "2001-01-01" @default.
- W102512913 modified "2023-09-27" @default.
- W102512913 title "Regulation of Cellular 5-Lipoxygenase Activity by Glutathione Peroxidases" @default.
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- W102512913 doi "https://doi.org/10.1007/978-94-015-9721-0_4" @default.
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