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Evidence for SLC7A11-dependent actin-protein disulfide bonding during UMRC6 glucose withdrawal
In cultured SLC7A11-high UMRC6 cancer cells, one-hour glucose withdrawal increased the NADP+/NADPH ratio, a redox indicator, without altered protein migration. At two hours, actin-cytoskeleton proteins showed slower migration and high-molecular-weight patterns on non-reducing Western blots; reducing conditions eliminated these patterns. SLC7A11 knockout abolished the withdrawal-induced migration change. The authors interpreted the pattern as intermolecular disulfide bonding. It appeared before obvious cell death, supporting—not proving—that bonding was not merely a consequence of dying cells. These controls and timing do not independently establish every causal step.
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