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Dominant-negative Jun N-terminal protein kinase (JNK-1) inhibits metabolic oxidative stress during glucose deprivation in a human breast carcinoma cell line
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Dominant-negative Jun N-terminal protein kinase (JNK-1) inhibits metabolic oxidative stress during glucose deprivation in a human breast carcinoma cell line

Yong J Lee, Sandra S Galoforo, Julia E Sim, Lisa A Ridnour, Jinah Choi, Henry Jay Forman, Peter M Corry and Douglas R Spitz
Free radical biology & medicine, Vol.28(4), pp.575-584
2000
DOI: 10.1016/S0891-5849(99)00267-1
PMID: 10719239

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Abstract

Signal transduction pathways involved in glucose deprivation-induced oxidative stress were investigated in human breast carcinoma cells (MCF-7/ADR). In MCF-7/ADR, glucose deprivation-induced prolonged activation of c-Jun N-terminal kinase (JNK1) as well as cytotoxicity and the accumulation of oxidized glutathione. Glucose deprivation also caused significant increases in total glutathione, cysteine, γ-glutamylcysteine, and immunoreactive proteins corresponding to the catalytic as well as regulatory subunits of γ-glutamylcysteine synthetase, suggesting that the synthesis of glutathione increased as an adaptive response. Expression of a catalytically inactive dominant negative JNK1 in MCF-7/ADR inhibited glucose deprivation-induced cell death and the accumulation of oxidized glutathione as well as altered the duration of JNK activation from persistent (>2 h) to transient (30 min). In addition, stimulation of glutathione synthesis during glucose deprivation was not observed in cells expressing the highest levels of dominant negative protein. Finally, a linear dose response suppression of oxidized glutathione accumulation was noted for clones expressing increasing levels of dominant negative JNK1 during glucose deprivation. These results show that expression of a dominant negative JNK1 protein was capable of suppressing persistent JNK activation as well as oxidative stress and cytotoxicity caused by glucose deprivation in MCF-7/ADR. These findings support the hypothesis that JNK signaling pathways may control the expression of proteins contributing to cell death mediated by metabolic oxidative stress during glucose deprivation. Finally, these results support the concept that JNK signaling-induced shifts in oxidative metabolism may provide a general mechanism for understanding the diverse biological effects seen during the activation of JNK signaling cascades.
Free radicals Glucose deprivation Glutathione metabolism JNK Oxidative stress Signal transduction γ-Glutamylcysteine synthetase

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