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• W2037221024 abstract "Although copper is an essential element, it shows cytotoxic effects when present in excessive amounts with the production of hydroxyl radicals, which can damage phospholipids and enzymes. This necessitates a tight cellular control mechanism for copper homeostasis including its uptake and removal. The high copper contents in the liver of tilapia make this fish a suitable model for the study of copper binding proteins (CBPs). The liver was dissected from tilapia injected with Cu2+ and cytosolic fractions were separated by using Superdex 75 column chromatography followed by atomic absorption spectrometry. Fractions in two major peaks containing CBPs were analyzed by using differential proteomic approaches, and loaded on a Cu chelating ion-immobilized affinity column (Cu-IMAC). Of the 113 differentially expressed proteins in these two peaks, 28 proteins were found to have copper binding ability, including well-characterized CBPs, such as copper transporter ATP7A and metallothionein. The networks of CBPs built up by Ingenuity Pathway Analysis (IPA) would help us to understand the transportation pathway and function of CBPs, which were related to free radical scavenging, cellular development and lipid metabolism. In addition, our results suggest that Cu2+ would compete with Fe2+ and Ca2+ in binding with some target proteins, such as ferritin, transferrin, and calmodulin. Copper binds not only to the copper transporter, metallothionein, but also to iron and calcium binding proteins, and other proteins controlling cellular growth and lipid metabolism." @default.
• W2037221024 created "2016-06-24" @default.
• W2037221024 creator A5034927596 @default.
• W2037221024 creator A5048734108 @default.
• W2037221024 date "2012-01-01" @default.
• W2037221024 modified "2023-10-14" @default.
• W2037221024 title "Identification of hepatic copper-binding proteins from tilapia by column chromatography with proteomic approaches" @default.
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• W2037221024 doi "https://doi.org/10.1039/c2mt20057k" @default.
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