Abstract Title:

Induction of apoptosis by luteolin through cleavage of Bcl-2 family in human leukemia HL-60 cells.

Abstract Source:

Eur J Pharmacol. 2005 Feb 10;509(1):1-10. Epub 2005 Jan 21. PMID: 15713423

Abstract Author(s):

An-Chin Cheng, Tzou-Chi Huang, Ching-Shu Lai, Min-Hsiung Pan

Article Affiliation:

Department of Food Science, National Pingtung University, 912, Pingtung, Taiwan.


In our study, luteolin has shown its apoptosis-inducing potent in HL-60 cells with its 76.5% apoptotic ratio of 100 microM treatment. When HL-60 cells were treated with 60 microM of luteolin, DNA ladders were visible at 6 h and increased from 6-12 h after treatment. Luteolin could decrease the mitochondrial membrane potential, trigger cytochrome c released to cytosol, and subsequently induce the processing of procaspase-9 and procaspase-3, which were followed by the cleavage of poly-(ADP-ribose) polymerase (PARP) and DNA fragmentation factor (DFF-45). The cleavage of the proapoptotic Bcl-2 proteins, such as Bad and Bax to produce their truncated forms, and the cleavage of the antiapoptotic Bcl-2 proteins, such as Bcl-2 and Bcl-XL, into their potent pro-apoptotic fragments were detected in our study. From the results, we suggested that the structure of luteolin contributes to its potent in inducing apoptosis in HL-60 cells, and the mitochondrial pathway might play an important role in the luteolin-induced apoptosis. The induction of apoptosis by luteolin may offer a pivotal mechanism for its cancertherapeutic and chemopreventive action.

Study Type : In Vitro Study

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