Challenges the widely accepted beneficial effects of the phytochemical. A major effect of CUR is its ability to both modulate and generate intracellular ROS, as reported in several tumor cell types. ROS in low amounts are implicated in regular cell function, signaling pathways, response to environmental stresses and carcinogenesis. In high amount, ROS cause DNA damage, lipid and protein peroxidation, and apoptosis. In this study, ROS balance between production and quenching could be evaluated from tail DNA measurement which accounts for DNA oxidative damage and effectiveness of DNA repair systems. Tail DNA increased at high doses, in favor that ROS production overwhelmed cellular quenching capacities at those doses. Also, some increase in ROS-related damages was found during delayed exposure to CUR used both alone and in combination with DTX. Among metabolites testifying DNA damage, 8-hydroxydeoxyguanosine is the most abundant and by far the most studied. But this biomarker of oxidative stress, as well as others including malonyldialdehyde, a product of lipid peroxidation, are Tulathromycin B beyond detectability in most NMR-based studies. However, in this study, an unusual product of glucose oxidation significantly increased at 25 mg.l21. This metabolite, Gna, has been reported to accumulate in breast cancer cells in a model of alkaloid-induced oxidative stress. Also, in this study, MCF7 and MDA-MB-231 breast cancer cells demonstrated the same major dose-dependent metabolic targets including glutathione metabolism and lipid metabolism. Because these cell types differ by their expression of hormonal receptors, it may be concluded that the reported major metabolic targets do not depend on hormonal signalling pathways, which make CUR a candidate adjuvant therapy for estrogen-negative breast tumors with lower prognosis. A prominent target of CUR is GSH metabolism, as revealed by GSx and GSx-related magnitude of changes. The main regulatory enzyme of GSH synthesis is glutamate-cysteine ligase. GSH plays a central role in cell protection against oxidative stress as a cofactor of GSH peroxidases and GST. GST enzymes belong to a family of multifunctional detoxification proteins that protect cells from electrophilic compounds. Overexpression of GST in cancer is implicated in multidrug resistance. However, intense conjugation and efflux may provoke GSH cellular depletion, impairment of detoxification, and cell death. In this study, changes in GSx and related metabolites LOUREIRIN-B testified of upregulated biosynthesis of GSH through activation of GCL at low doses explaining the enrolment of transsulfuration. Reactivation of GST at 50 mg.l21, at least in part, explained the drop of GSx levels, since both parameters correlate negatively and since biosynthetic activity of GSx was sustained. High levels of GSH have been reported in response to CUR, as well as upregulation of GCL. Another enzyme, cystathionine beta-synthase, which regulates transsulfuration, plays an important role in glutathione homeostasis. Our measurements, especially Hcy, show that CBS pathway was recruited to respond to dramatic requirement for GSH. GST activity was biphasic with decreased activity at low dose CUR then increased activity at high dose, in agreement with literature data. Overall, at high dose CUR, increased tail DNA, GST re-activation, GSx decrease, consistent changes in GSx-related metabolites, and Gna increase, together support the fact that ROS production.