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.
Copyright © 2011 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis / drug effects*
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Carcinoma / drug therapy
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Carcinoma / pathology
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Caspase 8 / metabolism
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Cell Proliferation / drug effects
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Cell-Penetrating Peptides / chemical synthesis
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Cell-Penetrating Peptides / pharmacology*
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DNA Fragmentation / drug effects
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Erythrocytes / drug effects
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Female
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Fibrosarcoma / drug therapy
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Fibrosarcoma / pathology
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Fish Proteins / chemical synthesis
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Fish Proteins / pharmacology*
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Fish Venoms / chemical synthesis
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Fish Venoms / pharmacology*
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Fishes, Poisonous / metabolism
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G1 Phase / drug effects
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HeLa Cells
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Humans
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Molecular Sequence Data
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Neurotoxins / chemical synthesis
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Neurotoxins / pharmacology*
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Organ Specificity
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Up-Regulation
Substances
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Cell-Penetrating Peptides
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Fish Proteins
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Fish Venoms
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Neurotoxins
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pardaxin
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Caspase 8