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Cross-resistance between cisplatin, antimony potassium tartrate, and arsenite in human tumor cells.

Journal article
Authors Peter Naredi
D D Heath
R E Enns
S B Howell
Published in The Journal of clinical investigation
Volume 95
Issue 3
Pages 1193-8
ISSN 0021-9738
Publication year 1995
Published at Institute of Surgical Sciences, Department of Surgery
Pages 1193-8
Language en
Keywords Anions, pharmacology, Antimony Potassium Tartrate, pharmacology, toxicity, Arsenites, metabolism, pharmacology, toxicity, Biological Transport, Carcinoma, Cisplatin, pharmacology, toxicity, Dose-Response Relationship, Drug, Drug Resistance, Multiple, physiology, Female, Head and Neck Neoplasms, Humans, Neoplasms, drug therapy, Organoplatinum Compounds, metabolism, pharmacology, Ovarian Neoplasms, Selection, Genetic, Tumor Cells, Cultured
Subject categories Cancer and Oncology


Cross-resistance between cisplatin (DDP) and metalloid salts in human cells was sought on the basis that mechanisms that mediate metalloid salt cross-resistance in prokaryotes are evolutionarily conserved. Two ovarian and two head and neck carcinoma cell lines selected for DDP resistance were found to be cross-resistant to antimony potassium tartrate, which contains trivalent antimony. The DDP-resistant variant 2008/A was also cross-resistant to arsenite but not to stibogluconate, which contains pentavalent antimony. A variant selected for resistance to antimony potassium tartrate was cross-resistant to DDP and arsenite. Resistance to antimony potassium tartrate and arsenite was of a similar magnitude (3-7-fold), whereas the level of resistance to DDP was greater (17-fold), irrespective of whether the cells were selected by exposure to DDP or to antimony potassium tartrate. In the resistant sublines, uptake of [3H]-dichloro(ethylenediamine) platinum(II) was reduced to 41-52% of control, and a similar deficit was observed in the accumulation of arsenite. We conclude that DDP, antimony potassium tartrate, and arsenite all share a common mechanism of resistance in human cells and that this is due in part to an accumulation defect.

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