过氧化物酶体
谷胱甘肽
谷胱甘肽
氧化还原
抗氧化剂
生物化学
化学
NAD+激酶
谷胱甘肽二硫化物
过氧化物酶体靶向信号
过氧化物酶体障碍
细胞生物学
酶
生物
受体
有机化学
作者
Cláudio F. Costa,Celien Lismont,Serhii Chornyi,Hongli Liu,Mohamed A. F. Hussein,Hans R. Waterham,Marc Fransen
出处
期刊:Antioxidants
[MDPI AG]
日期:2023-06-07
卷期号:12 (6): 1236-1236
被引量:4
标识
DOI:10.3390/antiox12061236
摘要
Peroxisomes serve as important centers for cellular redox metabolism and communication. However, fundamental gaps remain in our understanding of how the peroxisomal redox equilibrium is maintained. In particular, very little is known about the function of the nonenzymatic antioxidant glutathione in the peroxisome interior and how the glutathione antioxidant system balances with peroxisomal protein thiols. So far, only one human peroxisomal glutathione-consuming enzyme has been identified: glutathione S-transferase 1 kappa (GSTK1). To study the role of this enzyme in peroxisomal glutathione regulation and function, a GSTK1-deficient HEK-293 cell line was generated and fluorescent redox sensors were used to monitor the intraperoxisomal GSSG/GSH and NAD+/NADH redox couples and NADPH levels. We provide evidence that ablation of GSTK1 does not change the basal intraperoxisomal redox state but significantly extends the recovery period of the peroxisomal glutathione redox sensor po-roGFP2 upon treatment of the cells with thiol-specific oxidants. Given that this delay (i) can be rescued by reintroduction of GSTK1, but not its S16A active site mutant, and (ii) is not observed with a glutaredoxin-tagged version of po-roGFP2, our findings demonstrate that GSTK1 contains GSH-dependent disulfide bond oxidoreductase activity.
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