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Open AccessJournal ArticleDOI

Resistance of human tumor cells in vitro to oxidative cytolysis.

J O'Donnell-Tormey, +2 more
- 01 Jul 1985 - 
- Vol. 76, Iss: 1, pp 80-86
TLDR
Nine human cell types displayed a marked resistance to lysis by hydrogen peroxide, with both catalase and the GSH redox cycle inhibited, that is, resistance independent of detectable degradation of H2O2.
Abstract
Nine human cell types, six of them malignant, displayed a marked resistance to lysis by hydrogen peroxide (LD50, 2-20 mM). Of the reactive oxygen intermediates generated extracellularly, only H2O2 lysed all the cell types. OH was lytic to one of four, OI- to one of one, and O-2 to none of four cell types tested. Resistance to oxidative lysis did not correlate with specific activity of catalase, glutathione (GSH) peroxidase, other peroxidases, or glutathione disulfide reductase, or with specific content of GSH. Resistance to H2O2 seemed to occur via mechanisms distinct from those responsible for cellular consumption of H2O2. Consumption was inhibitable by azide and was probably due to catalase in each cell type. In contrast, resistance to oxidative lysis occurred via distinct routes in different cells. One cell type used the GSH redox cycle as the primary defense against H2O2, like murine tumors previously studied. Other cells seemed to utilize catalase as the major defense against H2O2. Nonetheless, with both catalase and the GSH redox cycle inhibited, all the human cells tested exhibited an inherent resistance to oxidative lysis, that is, resistance independent of detectable degradation of H2O2.

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References
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Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues

TL;DR: The use of the foregoing analytical method in the determination of total and oxidized glutathione contents of rat blood, kidney, and liver gave values in good agreement with those obtained by previous investigators.
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The Reduction of Cytochrome c by Milk Xanthine Oxidase

TL;DR: The data are consistent with the conclusion that xanthine oxidase generates an unstable reduced form of oxygen, presumably the superoxide anion, and that this radical is the agent which directly reduces cytochrome c and initiates the sulfite-oxygen chain reaction.
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Role of Superoxide dismutase in cancer: a review.

TL;DR: It is shown how diminished enzyme activities along with radical production may lead to many of the observed properties of cancer cells.
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Absence of HeLa Cell Contamination in 169 Cell Lines Derived From Human Tumors

TL;DR: Of 192 lines established in this or other laboratories, 169 lines were found to be G6PD type B; Twenty-three lines were type A as HeLa; three were of Negroid origin.
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Iodination of bacteria: a bactericidal mechanism

TL;DR: Iodination of the bacteria by the myeloperoxidase-iodide-H2O2 system was demonstrated chemically and radioautographically and suggests the involvement of labile intermediates of iodide oxidation rather than the more stable end products of oxidation such as iodine.
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