Overexpressed Mitochondrial Thioredoxin Protects PC12 Cells from Hydrogen Peroxide and Serum-deprivation.
- Author:
Yun Song LEE
1
;
Seung A YU
Author Information
1. Division of Pharmacology, Department of Molecular & Cellular Biology, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. yslee@yurim.skku.ac.kr
- Publication Type:Original Article
- Keywords:
Mitochondrial thioredoxin (Trx2);
Oxidative stress;
Serum deprivation;
PC12 cells;
Cell death
- MeSH:
Animals;
Catalytic Domain;
Cell Death;
Cysteine;
Humans;
Hydrogen Peroxide*;
Hydrogen*;
Mitochondria;
Oxidation-Reduction;
Oxidative Stress;
PC12 Cells*;
Serine;
Thioredoxins*
- From:The Korean Journal of Physiology and Pharmacology
2003;7(1):33-37
- CountryRepublic of Korea
- Language:English
-
Abstract:
Oxidative damage to mitochondria is a critical mechanism in necrotic or apoptotic cell death induced by many kinds of toxic chemicals. Thioredoxin (Trx) family proteins are known to play protective roles in organisms under oxidative stress through redox reaction by using reducing equivalents of cysteines at a conserved active site, Cys-X-X-Cys. Whereas biological and physiological properties of Trx1 are well characterized, significance of mitochondrial thioredoxin (Trx2) is not well known. Therefore, we addressed physiological role of Trx2 in PC12 cells under oxidative stress. In PC12 cells, transiently overexpressed Trx2 significantly reduced cell death induced by hydrogen peroxide, whereas mutant Trx2, having serine residues instead of two cysteine residues at the active site did not. In addition, stably expressed Trx2 protected PC12 cells from serum deprivation. These results suggest that Trx2 may play defensive roles in PC12 cells by reducing oxidative stress to mitochondria.
