Copper binding promotes the interaction of cisplatin with human copper chaperone Atox1.
نویسندگان
چکیده
Cu(I) binding promotes the platination of Atox1, although cisplatin binds to the copper coordination sites. In addition, Cu(I) binding enhances the competition of Atox1 with DTT in the reaction of cisplatin. These results indicate that cuprous ions could regulate the cellular trafficking of cisplatin.
منابع مشابه
Copper binding modulates the platination of human copper chaperone Atox1 by antitumor trans-platinum complexes.
The transport system of platinum-based anticancer agents is crucial for drug sensitivity. Increasing evidence indicates that the copper transport system is also involved in the cellular influx and efflux of platinum drugs. The copper chaperone Atox1 has been shown to bind to cisplatin in vitro and in cells. Previous results reveal that copper binding promotes the reaction between Atox1 and cisp...
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Cisplatin (cisPt), Pt(NH(3))(2)Cl(2), is a cancer drug believed to kill cells via DNA binding and damage. Recent work has implied that the cellular copper (Cu) transport machinery may be involved in cisPt cell export and drug resistance. Normally, the Cu chaperone Atox1 binds Cu(I) via two cysteines and delivers the metal to metal-binding domains of ATP7B; the ATP7B domains then transfer the me...
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Postprint This is the accepted version of a paper published in Protein peptide letters. This paper has been peer-reviewed but does not include the final publisher proof-corrections or journal pagination. Interaction between anticancer drug Cisplatin and copper chaperone Atox1 in human melanoma cells. Protein peptide letters Access to the published version may require subscription. Cisplatin (Ci...
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The human metallo-chaperone protein Atox1 features a high affinity Cu(I) binding site Cys(12)GlyGlyCys(15) (KD = 10(-17.4) M at pH 7.0) and delivers copper to the trans-Golgi network (TGN). Atox1 may participate in the metabolism of the drug cis-Pt(NH3)2Cl2 (cisplatin), either as a component of its delivery to the nucleus or of its loss via transport to the TGN and beyond. The species of stoich...
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ورودعنوان ژورنال:
- Chemical communications
دوره 49 95 شماره
صفحات -
تاریخ انتشار 2013