期刊
REDOX BIOLOGY
卷 10, 期 -, 页码 274-284出版社
ELSEVIER
DOI: 10.1016/j.redox.2016.10.010
关键词
-
资金
- National Institutes of Health (NIH) [R01 CA169046, R01 GM073929, T32 CA148062, P42 ES013661, P30 ES005605, R01 CA184051]
- Gateway for Cancer Research
- Holden Comprehensive Cancer Center [P30 CA086862]
Ascorbate (AscH-) functions as a versatile reducing agent. At pharmacological doses (P-AscH(-); [plasma AscH(-)] >=approximate to 20 mM), achievable through intravenous delivery, oxidation of P-AscH-can produce a high flux of H2O2 in tumors. Catalase is the major enzyme for detoxifying high concentrations of H2O2. We hypothesize that sensitivity of tumor cells to P-AscH-compared to normal cells is due to their lower capacity to metabolize H2O2. Rate constants for removal of H2O2 (kcell) and catalase activities were determined for 15 tumor and 10 normal cell lines of various tissue types. A differential in the capacity of cells to remove H2O2 was revealed, with the average kcell for normal cells being twice that of tumor cells. The ED50 (50% clonogenic survival) of P-AscH(-) correlated directly with kcell and catalase activity. Catalase activity could present a promising indicator of which tumors may respond to P-AscH-.
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