Hepcidin (TH1-5) is a cysteine-rich antimicrobial peptide originally isolated from the freshwater fish Oreochromis mossambicus. A synthesized form of the peptide has been reported to exhibit cytotoxic activity against few human cancer cell lines. This study investigated the potential cytotoxicity of the peptide against human breast cancer cell line and normal mouse embryonic fibroblast cell line (NIH/3T3) using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. Morphological changes by acridine orange and propidium iodide (AO/PI) double staining were also studied to determine apoptotic evidences. Hepcidin (TH1-5) showed cytotoxic activity against MCF7 with an IC50 of 20 mg/mL but no significant effect against NIH/3T3. This outcome indicates hepcidin (TH1-5) to be a promising cytotoxic peptide that warrants further studies as a potential anticancer agent for breast cancer therapy.
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-inducing effect of the cysteine-rich peptide in the present study. Annexin V-fluorescein isothiocyanate and propidium iodide (annexin V-FITC/PI) apoptosis assay was performed after treatment of the cells. In the determination of caspase activity and pathway of apoptosis, luminescent assay was also performed where caspase-3/7, caspase-8 and caspase-9 were evaluated. Results of annexin V-FITC/PI staining showed proportion of early apoptotic cell were 73.67 ± 4.93%, 61.00 ± 5.57% and 44.33 ± 2.52% at 24, 48 and 72 hours respectively, while late apoptotic cell were 6.33 ± 1.53%, 23 ± 3.56% and 34 ± 3.51% within the same time interval. Based on the data from the luminescence test, Hepcidin TH1-5 activated caspases-3/7 and -9 which suggests that the apoptosis induced was due to the peptide treatment. Hepcidin TH1-5 induced apoptosis in MCF-7 via the activation of caspase-9 of the intrinsic pathway. These results support our previous findings of the cytotoxicity of Hepcidin TH1-5 and indicate that the peptide may be a potential agent for breast cancer therapy.
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