Title : Glutathione peroxidase-1 overexpression prevents ceramide production and partially inhibits apoptosis in doxorubicin-treated human breast carcinoma cells.

Pub. Date : 2001 Sep

PMID : 11502879






5 Functional Relationships(s)
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1 Glutathione peroxidase-1 overexpression prevents ceramide production and partially inhibits apoptosis in doxorubicin-treated human breast carcinoma cells. Doxorubicin glutathione peroxidase 1 Homo sapiens
2 We selectively investigated the interaction of seleno-glutathione peroxidase-1 (GPx-1), the major enzyme responsible for peroxide detoxification in mammalian cells, with the cytotoxic response of T47D human breast cancer cells to doxorubicin, an anticancer drug known to promote production of ROS and apoptotic mediator ceramide. Doxorubicin glutathione peroxidase 1 Homo sapiens
3 We selectively investigated the interaction of seleno-glutathione peroxidase-1 (GPx-1), the major enzyme responsible for peroxide detoxification in mammalian cells, with the cytotoxic response of T47D human breast cancer cells to doxorubicin, an anticancer drug known to promote production of ROS and apoptotic mediator ceramide. Doxorubicin glutathione peroxidase 1 Homo sapiens
4 The glutathione precursor, N-acetylcysteine also partially protected T47D/H3 cells from the lethal effect of doxorubicin, whereas L-buthionine-(S,R)-sulfoximine, an inhibitor of glutathione biosynthesis, sensitized both GPx-1--deficient and -proficient cells. Doxorubicin glutathione peroxidase 1 Homo sapiens
5 Taken together, these results indicate that GPx-1 can regulate doxorubicin-induced cell death signaling at least in part by interfering with the activation of the sphingomyelin-ceramide pathway. Doxorubicin glutathione peroxidase 1 Homo sapiens