Overproduction of human Mn‐superoxide dismutase modulates paraquat‐mediated toxicity in mammalian cells

FEBS Letters

Ho, Ye-Shih¹  St. Clair, Daret K.³  Oberley, Terry D.² 

[1]Department of Medicine, Duke University Medical Center, Durham, North Carolina, USA

[2]Department of Pathology, University of Wisconsin-Madison, Madison, Wisconsin, USA

[3]Department of Radiology, Bowman Gray School of Medicine, Winston-Salem, North Carolina, USA

关键词: Superoxide dismutase;    Gene dosage;    Mitochondrion;    Oxidative stress;    Paraquat;   

DOI  :  10.1016/0014-5793(91)81186-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Manganese superoxide dismutase (MnSOD) is a nuclear encoded mitochondrial matrix enzyme that functions to scavenge superoxide radicals. The human MnSOD cDNA under the transcriptional control of a human β-actin promoter was introduced into mouse C3H10T cells by cotransfection with a recombinant plasmid containing the Neo^R selectable marker. C3H10T transformants (C3H-SOD) were obtained that expressed high levels of authentic enzymatically active human MnSOD. Overexpression of the MnSOD gene did not affect the protein levels of CuZnSOD, catalase (CAT), or glutathione peroxidase (GPX) in the transformants. Treatment of cells with paraquat was less toxic to the C3H-SOD cells than to the control cells. These results are consistent with the possibility that superoxide radicals are mediators of paraquat cytotoxicity.

【 授权许可】

Unknown