Peroxiredoxin III Protects Tumor Suppressor PTEN from Oxidation by 15-Hydroperoxy-eicosatetraenoic Acid
| Autor: | Iha Park, Hyun Ae Woo, Seung-Rock Lee, Jiyoung Park, Jong Suk Kim, Ying Zhang, Seong Jeong Han, Yongwoon Lim |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Aging
Leukotrienes Lipid Peroxides Peroxiredoxin III Article Subject Phosphatase Oxidative phosphorylation Transfection Biochemistry Lipid peroxidation chemistry.chemical_compound Mice PTEN Tensin Animals Humans lcsh:QH573-671 biology Lipid peroxide Chemistry lcsh:Cytology PTEN Phosphohydrolase Cell Biology General Medicine Cell biology biology.protein Thioredoxin Oxidation-Reduction Research Article |
| Zdroj: | Oxidative Medicine and Cellular Longevity, Vol 2019 (2019) Oxidative Medicine and Cellular Longevity |
| ISSN: | 1942-0900 |
| DOI: | 10.1155/2019/2828493 |
| Popis: | Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a lipid and protein phosphatase that coordinates various cellular processes. Its activity is regulated by the reversible oxidation of an active-site cysteine residue by H2O2and thioredoxin. However, the potential role of lipid peroxides in the redox regulation of PTEN remains obscure. To evaluate this, 15-hydroperoxy-eicosatetraenoic acid (15s-HpETE), a lipid peroxide, was employed to investigate its effect on PTEN using molecular and cellular-based assays. Exposure to 15s-HpETE resulted in the oxidation of recombinant PTEN. Reversible oxidation of PTEN was also observed in mouse embryonic fibroblast (MEF) cells treated with a 15s-HpETE and Lipofectamine mixture. The oxidative dimerization of thioredoxin was found simultaneously. In addition, the absence of peroxiredoxin III aggravated 15s-HpETE-induced PTEN oxidation in MEF cells. Our study provides novel insight into the mechanism linking lipid peroxidation to the etiology of tumorigenesis. |
| Databáze: | OpenAIRE |
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