Article ID Journal Published Year Pages File Type
2006428 Peptides 2011 7 Pages PDF
Abstract

Pardaxin, a pore-forming antimicrobial peptide that encodes 33 amino acids was isolated from the Red Sea Moses sole, Pardachirus mamoratus. In this study, we investigated its antitumor activity in human fibrosarcoma (HT-1080) cells and epithelial carcinoma (HeLa) cells. In vitro results showed that the synthetic pardaxin peptide had antitumor activity in these two types of cancer cells and that 15 μg/ml pardaxin did not lyse human red blood cells. Moreover, this synthetic pardaxin inhibited the proliferation of HT1080 cells in a dose-dependent manner and induced programmed cell death in HeLa cells. DNA fragmentation and increases in the subG1 phase and caspase 8 activities suggest that pardaxin caused HeLa cell death by inducing apoptosis, but had a different mechanism in HT1080 cells.

► Pardaxin induced apoptosis with treatment. ► Pardaxin inhibited tumor cell growth. ► DNA fragmentation and increases in the subG1 phase and caspase 8 activity suggest that pardaxin caused HeLa cell death by inducing apoptosis, but had a different mechanism in HT1080 cells.

Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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