Glutathione peroxidase and oxidative stress.
In this study, overexpression of the cDNA for the major cytoplasmic glutathione peroxidase isoenzyme, GSH Peroxidase 1 (GSHPx-1), in human MCF-7 breast cancer cells has been shown to significantly increase the tolerance of these cells to oxidative stress produced by hydrogen peroxide or by the redox cycling of the quinone-containing anticancer agent doxorubicin. These experiments suggest that intracellular detoxification of hydrogen peroxide by the glutathione-glutathione peroxidase cycle plays a critical role in resistance against oxidant stress produced by xenobiotics.
Doroshow
J H
JH
Department of Medical Oncology and Therapeutics Research, City of Hope National Medical Center, Duarte, CA 91010, USA.
D000975:Antioxidants / Q000032:analysis; D001943:Breast Neoplasms / Q000378:metabolism / Q000473:pathology; D004317:Doxorubicin / Q000633:toxicity; D005260:Female; D005979:Glutathione Peroxidase / Q000502:physiology*; D006801:Humans; D006861:Hydrogen Peroxide / Q000633:toxicity; D018384:Oxidative Stress; D014407:Tumor Cells, Cultured
D000975:Antioxidants; D004317:Doxorubicin; D006861:Hydrogen Peroxide; D005979:Glutathione Peroxidase