Evaluation of copper chaperone ATOX1 as prognostic biomarker in breast cancer
نویسندگان
چکیده
منابع مشابه
Conserved residues modulate copper release in human copper chaperone Atox1.
It is unclear how the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson and Menkes disease proteins in the cytoplasm. To begin to address this problem, we have characterized Cu(I) release from wild-type Atox1 and two point mutants (Met(10)Ala and Lys(60)Ala). The dynamics of Cu(I) displacement from holo-Atox1 were measured by using the Cu(I) chelator bicinchonic a...
متن کاملEvaluation of KiSS1 as a Prognostic Biomarker in North Indian Breast Cancer Cases.
BACKGROUND Breast cancer is the commonest female cancer worldwide and its propensity to metastasize negatively impacts on therapeutic outcome. Several clinicopathological parameters with prognostic/predictive significance have been associated with metastatic suppressor expression levels. The role of metastatic suppressor gene (MSG) KiSS1 in breast cancer remains unclear. Our goal was to investi...
متن کاملThe Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution
Human antioxidant protein 1 (Atox1) is a small cytosolic protein with an essential role in copper homeostasis. Atox1 functions as a copper carrier facilitating copper transfer to the secretory pathway. This process is required for activation of copper dependent enzymes involved in neurotransmitter biosynthesis, iron efflux, neovascularization, wound healing, and regulation of blood pressure. Re...
متن کاملCopper 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...
متن کاملCopper binding promotes the interaction of cisplatin with human copper chaperone Atox1.
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.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Breast Cancer
سال: 2020
ISSN: 1340-6868,1880-4233
DOI: 10.1007/s12282-019-01044-4