| Literature DB >> 21557975 |
Jung-Chieh Hsu1, Li-Ching Lin, Jason T C Tzen, Jyh-Yih Chen.
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 15μg/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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 21557975 DOI: 10.1016/j.peptides.2011.04.024
Source DB: PubMed Journal: Peptides ISSN: 0196-9781 Impact factor: 3.750