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. 2021 Dec 14;23(2):47. doi: 10.3892/ol.2021.13165

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Copyright: © Tang et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 1. — Structure and function of Xc-. The Xc- system consists of two subunits, namely, light (SLC7A11) and heavy (SLC3A2) chain subunits. SLC7A11 exerts the main biological function and transport activity, whereas SLC3A2 only participates in maintaining the stability of SLC7A11 as a chaperone protein. SLC7A11 transfers a molecule of extracellular cystine into the cell while transferring a molecule of intracellular glutamate out of the cell. The cystine transported into the cell is quickly reduced to cysteine. Next, cysteine and glutamic acid are combined under the action of GCL to form γ-glutamyl cysteine, and glycine is added to the C-terminus of γ-Glu-Cys through GS to produce reduced GSH. GPX4 then reduces lipid hydroperoxides into lipid alcohols through GSH, thereby inhibiting ferroptosis. At this time, GSH is oxidized into GSSG, which can be reduced to GSH again through GR. GCL, glutamate cysteine ligase; GS, glutathione synthetase; GPX4, glutathione peroxidase 4; GR, glutathione reductase; GSH, reduced glutathione; GSSG, oxidized glutathione; L-OOH, lipid hydroperoxide; L-OH, lipid alcohol; ROS, reactive oxygen species; SLC7A11, solute carrier family 7 member 11; SLC3A2, solute carrier family 3 member 2.