Research paperCollateral sensitivity to the bisdioxopiperazine dexrazoxane (ICRF-187) in etoposide (VP-16)-resistant human leukemia K562 cells☆,☆☆
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Structure-based design, synthesis and biological testing of piperazine-linked bis-epipodophyllotoxin etoposide analogs
2015, Bioorganic and Medicinal ChemistryCitation Excerpt :The extraction and purification of recombinant full-length human topoisomerase IIα were described previously.38 Human leukemia K562 cells, obtained from the American Type Culture Collection, and K/VP.5 cells (a 26-fold etoposide-resistant K562-derived sub-line with decreased levels of topoisomerase IIα mRNA and protein)29 were maintained as suspension cultures in αMEM (Invitrogen, Burlington, Canada) containing 10% fetal calf serum. The spectrophotometric 96-well plate 72 h cell growth inhibition MTS assay (Promega, Madison, WI) has been described previously.14,33
The anticancer multi-kinase inhibitor dovitinib also targets topoisomerase i and topoisomerase II
2012, Biochemical PharmacologyCitation Excerpt :Yeast topoisomerase II was expressed for purification using the plasmid pGAL1TOP2 [23] and induction of topoisomerase II by galactose as described [24]. Human leukemia K562 cells, obtained from the American Type Culture Collection and K/VP.5 cells (a 26-fold etoposide-resistant K562-derived sub-line with decreased levels of topoisomerase IIα mRNA and protein) [25] were maintained as suspension cultures in αMEM (Minimal Essential Medium Alpha) (Invitrogen, Burlington, Canada) containing 10% fetal calf serum. The spectrophotometric 96-well plate cell growth inhibition 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium (MTS) CellTiter 96 AQueous One Solution Cell Proliferation assay (Promega, Madison, WI), which measures the ability of the cells to enzymatically reduce MTS after drug treatment, has been described [26].
Cadmium is a catalytic inhibitor of DNA topoisomerase II
2011, Journal of Inorganic BiochemistryCitation Excerpt :The fact that the IC50 increased 11-fold when the treatment was carried out in the presence of 2 mM GSH suggests that GSH may be able to slow the entry of Cd2+ into the cells by its ability to form a complex and thereby restrict transport capacity. To determine whether Cd2+ was a topoisomerase IIα poison we investigated cadmium chloride-induced DNA double strand breaks and cross resistance to K/VP.5 cells, a K562-derived cell line with decreased levels of topoisomerase IIα mRNA and protein that is 26-fold resistant to the topoisomerase II poison etoposide [29]. While the K/VP.5 cells were only slightly cross-resistant to cadmium chloride (Fig. 3), cadmium chloride treatment of purified topoisomerase IIα did not induce formation of DNA double strand breaks (Fig. 2).
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This work was supported, in part, by Grant DHP-125 from the American Cancer Society and Leukemia Society of America Translational Research Grant 6238-95.
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This work was supported by N.LH. Grants NS 26511 and NS 30882. F. J. E. is a recipient of a United States Public Health Service Research Career Development Award (NS01396) from the National Institute of Neurological Disorders and Stroke.