Abstract
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. Recently, new cellular roles for Atox1 have emerged. Changing levels of Atox1 were shown to modulate response to cancer therapies, contribute to inflammatory response, and protect cells against various oxidative stresses. It has also become apparent that the activity of Atox1 is tightly linked to the cellular redox status. In this review, we summarize biochemical information related to a dual role of Atox1 as a copper chaperone and an antioxidant. We discuss how these two activities could be linked and contribute to establishing the intracellular copper balance and functional identity of cells during differentiation.
Highlights
Copper is the major redox-active element in most biological systems
Copper is utilized in many essential cellular processes including energy production by the respiratory chain, biosynthesis and degradation of neurotransmitters, formation of collagen matrix, redox signaling in angiogenesis, and removal of superoxide
We summarize available experimental data that suggest that the two antioxidant protein 1 (Atox1) functions might be coupled
Summary
Copper is the major redox-active element in most biological systems. As a redox catalyst, copper is utilized in many essential cellular processes including energy production by the respiratory chain, biosynthesis and degradation of neurotransmitters, formation of collagen matrix, redox signaling in angiogenesis, and removal of superoxide. It was established that the copper-binding site of Atox is sensitive to cytosolic redox environment [7,8] and that changes in the Atox levels may contribute to inflammatory response and antioxidant defense [9,10]. These observations suggest the role for Atox in a cellular redox balance or response to oxidative stress, but up to this day, it remains unclear whether antioxidant role is a derivative of the Atox copper-shuttling function or these two activities are mechanistically distinct. We summarize available experimental data that suggest that the two Atox functions might be coupled
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