Menadione effect on l-cysteine desulfuration in U373 cells.
Author(s) -
Maria Wróbel,
Halina Jurkowska
Publication year - 2007
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2007_3263
Subject(s) - menadione , glutathione , chemistry , rhodanese , cysteine , sulfurtransferase , sulfur , oxidative stress , biochemistry , reactive oxygen species , incubation , thiol , enzyme , cytotoxic t cell , in vitro , organic chemistry
The non-cytotoxic concentration (20 microM) of menadione (2-methyl-1,4-naphthoquinone), after 1 h of incubation, leads to loss of the activity of rhodanese by 33%, 3-mercaptopyruvate sulfurtransferase by 20%, as well as the level of sulfane sulfur by about 23% and glutathione by 12%, in the culture of U373 cells, in comparison with the control culture. Reactive oxygen species generated by menadione oxidize sulfhydryl groups in active centers of the investigated enzymes, inhibiting them and saving cysteine for glutathione synthesis. A decreased sulfane sulfur level can be correlated with an oxidative stress.
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