Effects of Mzb1 regulation by puerarin on endoplasmic reticulum stress-mediated mitochondrial dysfunction in cardiomyocytes
Objective To observe the effect of puerarin on the mitochondrial function in cardiomyocytes induced by tunicamycin.Methods AC 16 human cardiomyocytes were cultured.The endoplasmic reticulum stress was induced by tunicamycin.Puerarin was applied to cardiomyocytes.siRNA Mzb1(si-Mzb1)was transfected by Lipofectamine® 3000 liposomes.MTT assay was used to detect cell viability.ATP kit was used to detect changes in ATP content within each group.JC-1 staining was used to detect changes in mitochondrial membrane potential.Protein blotting was used to detect the expression level of marginal zone B and B1 cell-specific protein(Mzb1)and endoplasmic reticulum stress-related proteins,including glucose-regulated protein 78(GRP78)and CCAAT/enhancer-binding protein homologous protein(CHOP).Results Compared with the control group,tunicamycin induced a decrease in cell viability(P＜0.01),an increase in the expression of endoplasmic reticulum stress-related proteins GRP78 and CHOP(P＜0.05,P＜0.01),a significant decrease in the expression of Mzb1(P＜0.05),and a decrease in the ATP content and mitochondrial membrane potential(all P＜0.05).Compared with the tunicamycin group,the cell viability was elevated(P＜0.05),the expression of GRP78 and CHOP proteins was decreased(all P＜0.05),the expression of Mzb1 was elevated(P＜0.05),and the ATP content and mitochondrial membrane potential were partially restored(all P＜0.05)in the puerarin group.However,the effect of puerarin was blocked after the transfection of si-Mzb1(all P＜0.05).Conclusion Puerarin regulates Mzb1 to improve the endoplasmic reticulum stress-induced mitochondrial dysfunction in cardiomyocytes.
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