Proteomic analysis reveals ATP-dependent steps and chaperones involvement in luteolin-induced lung cancer CH27 cell apoptosis

Abstract

The present study applied 2D electrophoresis to analyze the proteins involved in luteolin (50 microM)-induced CH27 cell apoptosis. We found 7 proteins to be markedly changed. According to the data of analysis of these protein spots, we hypothesized that ATP synthetic pathway and heat shock proteins were involved in luteolin-induced CH27 cell apoptosis. In this study, luteolin induced a significant change in intracellular ATP levels and mitochondrial activity of CH27 cells. Further experiments demonstrated that pretreatment with forskolin blocked the luteolin-induced cell death. P38 and heat shock protein 27 may be important participants in the luteolin-induced changes in organization of actin microfilaments in this study. In addition, endoplasmic reticulum stress is also important in the luteolin-induced CH27 cell apoptosis. Our findings suggested that the function of mitochondria and endoplasmic reticulum is the integral factor in luteolin-induced CH27 cell apoptosis.