1997 Fiscal Year Final Research Report Summary
Regulation on new regulation in photoreceptor signal transduction
Grant-in-Aid for Scientific Research (C)
|Allocation Type||Single-year Grants |
|Research Institution||Okayama University |
TSUBOI Seiji Okayama University, Associate Prof., 薬学部, 助教授 (50172052)
OTSUKA Masato Okayama University, Res.Assoc., 薬学部, 助手 (30243489)
OHMORI Shinji Okayama Unviersity, Professor, 薬学部, 教授 (10032872)
|Project Period (FY)
1996 – 1997
|Keywords||glutathione / S- (12 -dicarboxyethyl) glutathione / acetoaminophen / hepatotoxicity / g-glutamylcysteine synthetase / yeast / cysteine / cystathionine b-synthetase|
(1) Protective effect of S- (1,2-dicarboxyethyl) glutathione (DCE-GS) and its esters on acetoaminophen-induced hepatotoxicity in rats
The pretreatment of DCE-GS triester prevented acetoaminophen-induced hepatotoxicity. It was found that the DCE-GS triester administration inhibited the GSH depletion caused by acetoaminophen, suggesting that the protective effect of DCE-GS triester on acetoaminophen-induced hepatotoxicity was due to the retention of hepatic GSH level.
(2) Elevation effect of DCE-GS triester on glutathione level
The effect of DCE-GS on GSH synthesis, especially g-glutamylcysteine synthetase, was studied in rat liver homogenate. In conclusion, DCE-GS promoted the hepatic GSH synthesis due to activation g-glutamylcysteine synthetase.
(3) DCE-GS in Yeast
DCE-GS was found in Saccharomyces cerevisiae. The DCE-GS synthesizing enzyme was purified from yeast. The molecular mass of the enzyme was 49 kDa.
(4) Contents of cysteine, glutathione and their related comounds as well as related enzyme activities in Saccharomyces serevisiae cultured under aerobic and anaerobic ocnditions
Yeast grown aerobically increased activities of defensive enzymes against an oxygen stress like catalase and superoxide dismutase, and levels of the protective comounds cysteine and glutathione. The elevated synthesis of glutathione could be associated to the increased levels of cysteine which in its turn was found to be controlled by the oxygen dependent activation o cystathionie b-synthetase
Research Products (6 results)