期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 452, 期 2, 页码 165-173出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2006.04.006
关键词
glutathione S-transferases; glutathione; lipid peroxidation; small cell lung cancer; doxorubicin; apoptosis
资金
- NCI NIH HHS [CA77495] Funding Source: Medline
- NIEHS NIH HHS [ES007754, ES012171, ES06676] Funding Source: Medline
It has been suggested that the a-class glutathione S-transferases (GSTs) protect various cell types from oxidative stress and lipid peroxidation (LPO). In order to examine the protective role of alpha-class GST isozyme hGSTA1-1 against doxorubicin (DOX)-induced lipid peroxidation, cytotoxicity, and apoptosis, human small cell lung cancer (SCLC) H69 cells were stably transfected with hGSTA1 Immunological and biochemical characterization of hGSTA1-transfected cells revealed the expression of functionally active hGSTA1-1 localized near the cellular plasma membranes. hGSTA1-transfected cells acquired significantly increased resistance to the DOX-induced cytotoxicity by suppressing lipid peroxidation levels in these cells. Overexpression of hGSTA1-1 in cells inhibited DOX-mediated depletion of GSH and higher GSH levels were found in DOX-treated hGSTA1-transfected cells as compared with empty vector-transfected controls. hGSTA1-1 overexpression also provided protection to cells from DOX-induced apoptosis by inhibiting phosphorylation of c-Jun-N-terminal kinases (JNK), caspase-3 activation, and by preserving the levels of anti-apoptotic protein Bcl-2. These results are consistent with the idea that the alpha-class GSTs provide protection against oxidative stress by attenuating lipid peroxidation and these enzymes can modulate signaling for apoptosis. (c) 2006 Elsevier Inc. All rights reserved.
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