1995
DOI: 10.1016/0891-5849(94)00188-p
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Ascorbic acid and cell survival of adriamycin resistant and sensitive MCF-7 breast tumor cells

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Cited by 36 publications
(16 citation statements)
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“…a Reactions were done at 30°C and contained 0.5 mM GSH, 0. tein glutathionylation is not yet known, however, it is possible that glutathionylation acts to protect cellular proteins by reversibly binding to sensitive sulfhydryls during times of oxidative stress [1]. Recently was reported [20] that TTase levels are lower in a variety of chemically transformed cells when compared to the untransformed cell type, suggesting that variations in TTase levels may have important cellular consequences. The creation of mammalian cell lines that over-and under-express TTase will provide an experimental paradigm in which the cellular functions of TTase can be studied more directly, including the effect TTase has on protein glutathionylation.…”
Section: Discussionmentioning
confidence: 99%
“…a Reactions were done at 30°C and contained 0.5 mM GSH, 0. tein glutathionylation is not yet known, however, it is possible that glutathionylation acts to protect cellular proteins by reversibly binding to sensitive sulfhydryls during times of oxidative stress [1]. Recently was reported [20] that TTase levels are lower in a variety of chemically transformed cells when compared to the untransformed cell type, suggesting that variations in TTase levels may have important cellular consequences. The creation of mammalian cell lines that over-and under-express TTase will provide an experimental paradigm in which the cellular functions of TTase can be studied more directly, including the effect TTase has on protein glutathionylation.…”
Section: Discussionmentioning
confidence: 99%
“…Paradoxically, anticancer activity of very high doses of intravenous ascorbate is most likely based on prooxidant effects via H 2 O 2 formation through autoxidation that occurs in the extracellular fluid but not in whole blood, indicating that ascorbate at chemotherapeutic concentrations in blood serves as a prodrug for H 2 O 2 delivery to tissue (62)(63)(64). It is also possible that, after spontaneous oxidation of ascorbate to the semidehydroascorbyl free radical, chemical dismutation generates ascorbic acid and dehydroascorbic acid, the oxidized form of ascorbate actively transported into cells and transformed to ascorbic acid in a reductive enzymatic process that is glutathione-dependent and may therefore induce cellular glutathione depletion (367). Indeed, ascorbic acidinduced glutathione depletion enhances As 2 O 3 induced apoptosis in animal models of lymphoma and leukemia, and the minimal toxicity of infusional ascorbic acid compares favorably with other glutathione-depleting agents discussed below (18,135).…”
Section: H Sacrificial Antioxidants: L-ascorbatementioning
confidence: 99%
“…In theory, the most straightforward way to modulate Grx activity in situ is to change the content of active enzyme by altering rates of its production or degradation. Although little is known about the transcriptional regulation of Grx1, some hormonal and metabolic stimuli are associated with increased protein content and activity, including doxorubicin (Adriamycin) treatment of MCF-7 breast cancer cells (140), estradiol treatment of cardiomyoblasts (134), MPTP exposure in male mice (63), and culture of retinal Mü ller cells in high-glucose media (115). Recently, Grx2 mRNA was found to be elevated in peripheral blood mononuclear cells treated with the antitumor agent imexon (6), presumably via a putative antioxidant response element (ARE) in its promoter sequence.…”
Section: Enzyme Concentrationmentioning
confidence: 99%