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J Cell Physiol. 2019 Apr;234(4):5117-5133. doi: 10.1002/jcp.27322. Epub 2018 Sep 7.

Heat-shock protein B1 upholds the cytoplasm reduced state to inhibit activation of the Hippo pathway in H9c2 cells.

Liu X1,2, Liu K1,2, Li C1,2, Cai J1,2, Huang L1,2, Chen H1,2, Wang H1,2, Zou J1,2, Liu M1,2, Wang K1,2, Tan S1,2, Zhang H1,2.

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Department of Pathophysiology, Xiangya School of Medicine, Central South University, Hunan, China.
Sepsis Translational Medicine Key Lab of Hunan Province, Central South University, Hunan, China.


Heat-shock protein B1 (HSPB1) is a multifunctional protein that protects against oxidative stress; however, its function in antioxidant pathways remains largely unknown. Here, we sought to determine the roles of HSPB1 in H9c2 cells subjected to oxidative stress. Using nonreducing sodium dodecyl sulfate polyacrylamide gel electrophoresis, we found that increased HSPB1 expression promoted the reduced states of glutathione reductase (GR), peroxiredoxin 1 (Prx1), and thioredoxin 1, whereas knockdown of HSPB1 attenuated these responses following oxidative stress. Increased HSPB1 expression promoted the activation of GR and thioredoxin reductase. Conversely, knockdown of HSPB1 attenuated these responses following oxidative stress. Importantly, overexpression of HSPB1 promoted the complex formation between HSPB1 and oxidized Prx1, leading to dephosphorylation of STE-mammalian STE20-like kinase 1 (MST1) in H9c2 cells exposed to H2 O 2 , whereas downregulation of HSPB1 induced the opposite results. Mechanistically, HSPB1 regulated the Hippo pathway by enhancing the dephosphorylation of MST1, resulting in reduced phosphorylation of LATS1 and Yes-associated protein (YAP). Moreover, HSPB1 regulated YAP-dependent gene expression. Thus, HSPB1 promoted the reduced state of endogenous antioxidant pathways following oxidative stress in H9c2 cells and improved the redox state of the cytoplasm via modulation of the Hippo signaling pathway.


antioxidants; heat-shock protein B1 (HSPB1); oxidation-reduction; oxidative stress; signal transduction


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