Title |
Glutathione Content and the Activities of GlutathioneSynthesizing Enzymes in Fission Yeast are Modulated by Oxidative Stress |
Author |
Yuk-Young Lee 1 , Su-Jung Kim 1 , Eun-Hee Park 2 , and Chang-Jin Lim 1 , * |
Address |
1 Division of Life Sciences, Kangwon National University, Chuncheon 200-701, Korea ; 2 College of Pharmacy, Sookmyung Womens University, Seoul 140-742, Korea(Received March 28, 2003 / Accepted June 12, 2003) |
Bibliography |
Journal of Microbiology, 41(3),248-251, 2003,
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DOI |
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Key Words |
tert-butylhydroquinone, [gamma]-glutamylcysteine synthetase, glutathione, glutathione synthetase, hydrogen peroxide, [beta]-naphthoflavone, Schizosaccharomyces pombe |
Abstract |
Glutathione (GSH) is an important factor in determining tolerance against oxidative stress in living organisms. It is synthesized in two sequential reactions catalyzed by [gamma]-glutamylcysteine synthetase (GCS) and glutathione synthetase (GS) in the presence of ATP. In this work, the effects of three different oxidative stresses were examined on GSH content and GSH-related enzyme activities in the fission yeast Schizosaccharomyces pombe. GSH content in S. pombe was significantly enhanced by treatment with hydrogen peroxide, [beta]-naphthoflavone (BNF) and tert-butylhydroquinone (BHQ). Simultaneously, they greatly induced GCS and GS activity. However, they did not have any effects on glutathione reductase activity. These results suggest that GCS and GS activities in S. pombe are upregulated by oxidative stress. |
Download PDF |
413-01.pdf |