HYDROGEN-PEROXIDE DEGRADATION AND GLUTATHIONE-PEROXIDASE ACTIVITY IN CULTURES OF THYROID-CELLS

被引:55
作者
BJORKMAN, U [1 ]
EKHOLM, R [1 ]
机构
[1] GOTHENBURG UNIV, DEPT ANAT & CELL BIOL, S-41390 GOTHENBURG, SWEDEN
关键词
HYDROGEN PEROXIDE DEGRADATION; GLUTATHIONE PEROXIDASE; CATALASE; SELENIUM; TSH; THYROID CELL CULTURE;
D O I
10.1016/0303-7207(95)03552-I
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The degradation rate of H2O2, added to the incubation medium, and glutathione (GSH) peroxidase activity were measured in cultures of FRTL-5 cells and porcine thyroid cells. The H2O2 degradation rate increased proportionally to the H2O2 concentration and was in FRTL-5 cells, cultured with TSH, similar to 50 nmol/min and mg DNA at 0.01 mM H2O2 and similar to 3 x 10(4) nmol/min and mg DNA at 10 mM H2O2. The GSH peroxidase activity in the same cells was equivalent to an H2O2 degradation of similar to 400 nmol/min and mg DNA. The involvement of enzymes in H2O2 degradation was studied by inhibiting catalase with aminotriazole (ATZ) and reducing GSH peroxidase by omitting glucose in the incubation medium. At 0.1 mM H2O2, ATZ or glucose omission alone did not measurably reduce H2O2 degradation but did so when combined. At 10 mM H2O2 ATZ caused a clear inhibition whereas glucose omission had no additive effect. These observations indicate that GSH peroxidase was involved in H2O2 degradation only at low H2O2 concentrations. The GSH peroxidase activity decreased by reduction of the selenite supply and increased after replenishment. The recovery of the enzyme activity required the presence of TSH in FRTL-5 calls but not in porcine thyrocytes.
引用
收藏
页码:99 / 107
页数:9
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