Breast cancer is the most commonly diagnosed and leading cause of cancer deaths among women globally. In continuation of our investigation into the cytotoxicity of the antimicrobial peptide, hepcidin TH1-5, on human breast adenocarcinoma cell line (MCF-7), we further affirm the apoptosis induction effect of the cysteine-rich antimicrobial peptide in the present study. Annexin V-fluorescein isothiocyanate and propidium iodide (annexin V-FITC/PI) apoptosis assay was carried out after treatment of the cells. In the determination of caspase activity and pathway of apoptosis, luminescence assay was also performed where caspase-3/7, caspase-8 and caspase-9 were evaluated at time 12, 24 and 48 hours. Results of annexin V-FITC/PI staining showed that 44.33%, 34.33%, 9.67% of the cell were in the early apoptosis, late apoptosis and necrotic stages respectively after 72 hours of treatment. Based on the data from the luminescence test, hepcidin TH1-5 activates caspases-3/7 and -9 which suggests that the apoptosis induced may be due to the peptide treatment. Hepcidin TH1-5 may have induced apoptosis in MCF-7 cells via the activation of caspase-9 of the intrinsic pathway. These results support our previous findings of the cytotoxicity of hepcidin TH1-5 and indicated that the peptide may be a potential agent for breast cancer therapy.
Key words: Hepcidin TH1-5, apoptosis, caspase, intrinsic, MCF-7
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