Role of mitochondrial oxidative stress in the apoptosis induced by diospyrin diethylether in human breast carcinoma (MCF-7) cells

2008 ◽  
Vol 320 (1-2) ◽  
pp. 185-195 ◽  
Author(s):  
Binod Kumar ◽  
Amit Kumar ◽  
B. N. Pandey ◽  
K. P. Mishra ◽  
Banasri Hazra
Keyword(s):  
Oxidative Stress ◽  
Breast Carcinoma ◽  
Human Breast Carcinoma ◽  
Human Breast ◽  
Mitochondrial Oxidative Stress ◽  
Mcf 7

scholarly journals Estradiol Exposure Differentially Alters Monolayer versus Microtissue MCF-7 Human Breast Carcinoma Cultures

PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0157997 ◽  
Author(s):  
Marguerite M. Vantangoli ◽  
Samantha J. Madnick ◽  
Shelby Wilson ◽  
Kim Boekelheide
Keyword(s):  
Breast Carcinoma ◽  
Human Breast Carcinoma ◽  
Human Breast ◽  
Mcf 7

scholarly journals Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

1994 ◽  
Vol 302 (3) ◽  
pp. 649-654 ◽  
Author(s):  
Z Kiss ◽  
M Tomono ◽  
W B Anderson
Keyword(s):  
Breast Carcinoma ◽  
Phospholipase D ◽  
Multidrug Resistant ◽  
Carcinoma Cells ◽  
Human Breast Carcinoma ◽  
Human Breast ◽  
Breast Carcinoma Cells ◽  
Human Breast Carcinoma Cells ◽  
Hydrolysis Of ◽  
Mcf 7

The phospholipase D (PLD)-mediated synthesis of phosphatidylethanol (PtdEtOH) and the hydrolysis of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) were examined in drug-sensitive and multidrug-resistant lines of MCF-7 human breast carcinoma cells. In drug-sensitive (MCF-7/WT) cells, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) failed to enhance either the synthesis of PtdEtOH or the hydrolysis of either phospholipid. In the drug-resistant (MCF-7/MDR) cells, 100 nM PMA greatly enhanced both the synthesis of PtdEtOH (approximately 21-fold) and the hydrolysis of PtdEtn (approximately 29-fold), but had no effect on the hydrolysis of PtdCho. The PLD activators sphingosine and H2O2 were found to elicit only a slight (1.28-1.4-fold) stimulatory effect on PtdCho hydrolysis in both the MCF-7/WT and MCF-7/MDR cell types, and had only a small effect on PtdEtn hydrolysis in the MCF-7/WT cells as well. However, these agents significantly (approximately 2.6-3.5-fold) stimulated PtdEtn hydrolysis in the MCF-7/MDR cells. These data indicate that MCF-7/MDR cells contain a PtdEtn-specific PLD activity which can be selectively stimulated by PMA, sphingosine and H2O2.

beta-Carotene is Accumulated, Metabolized, and Possibly Converted to Retinol in Human Breast Carcinoma Cells (MCF-7)

2004 ◽  
Vol 74 (3) ◽  
pp. 171-177 ◽  
Author(s):  
Torres ◽  
Borojevic ◽  
Trugo
Keyword(s):  
Breast Carcinoma ◽  
Beta Carotene ◽  
Human Breast Carcinoma ◽  
Breast Carcinoma Cell Line ◽  
Human Breast ◽  
Cell Extracts ◽  
Human Breast Carcinoma Cells ◽  
Dose Dependent ◽  
Mcf 7 ◽  
In Cells

The aims of the present study were to investigate the uptake, accumulation, and metabolism of beta-carotene by the human breast carcinoma cell line MCF-7. Beta-carotene uptake was time- and dose-dependent, and independent of cell polarity. Beta-carotene accumulation in cells was linear as a function of its concentration in medium (1.3–4.1 mumol/L). It was accompanied by increasing amounts of retinol, which accumulated in cells following a sigmoid pattern, and by other four putative metabolites. Beta-apocarotenals, epoxides, endoperoxides, retinal, retinoic acid, and retinyl esters were not detected in cell extracts. Beta-carotene and its metabolites did not induce alterations in cell morphology or subcellular localization of epithelial mucins. Beta-carotene and retinol were released from cells that had previously accumulated beta-carotene, and were further incubated in beta-carotene- and retinol-free medium, but intracellular retinol content remained constant whereas b-carotene decreased. In conclusion, beta-carotene added to culture medium in physiological concentrations (1–6 mumol/L) is taken up and metabolized in MCF-7 cells, and is possibly converted to retinol.

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