It has been reported that p62 is an interacting partner of Keap1, and that ectopic expression of p62 can result in the inhibition of Keap1-mediated Nrf2 ubiquitination and its subsequent degradation by the proteasome.38 In this regard, we showed that ESI could augment the interaction between Keap1 and p62, attenuate the binding of Keap1 to Nrf2, which allows Nrf2 to release from Keap1-Nrf2 complex and translocate to nuclear for activating target genes, such as p62 and HO-1.36 Our results indicate a positive feedback loop of Nrf2-p62-Keap1 driven by ESI in lung cancer cells. This evidence concerns the gene HMOX1 and lung carcinoma.