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  1. Article ; Online: Pardaxin, an antimicrobial peptide, triggers caspase-dependent and ROS-mediated apoptosis in HT-1080 cells.

    Huang, Tsui-Chin / Lee, Jheng-Fong / Chen, Jyh-Yih

    Marine drugs

    2011  Volume 9, Issue 10, Page(s) 1995–2009

    Abstract: Pardaxin is an antimicrobial peptide (AMP) that was first isolated from secretions of the Red Sea Moses sole. The role of pardaxin in inducing apoptosis for preventing cancer has not yet been investigated. In the present study, we examined the antitumor ... ...

    Abstract Pardaxin is an antimicrobial peptide (AMP) that was first isolated from secretions of the Red Sea Moses sole. The role of pardaxin in inducing apoptosis for preventing cancer has not yet been investigated. In the present study, we examined the antitumor activity of pardaxin against human fibrosarcoma HT-1080 cells; pardaxin inhibited cell proliferation by inducing apoptosis, as demonstrated by an increase in the externalization of plasma membrane phosphatidylserine and the presence of chromatin condensation. Additionally, pardaxin-treated cells showed elevation of caspase-3/7 activities, disruption of the mitochondrial membrane potential, and accumulation of reactive oxygen species (ROS) production. Inhibition of ROS production and caspase-3/7 activities reduced pardaxin-induced effects. Taken together, these findings suggest that pardaxin may be a potential anticancer agent for selectively inducing apoptosis in cancer cells.
    MeSH term(s) Antimicrobial Cationic Peptides/pharmacology ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Caspase 3/metabolism ; Caspase 7/metabolism ; Cell Line, Tumor/drug effects ; Cell Proliferation/drug effects ; Fibrosarcoma/drug therapy ; Fish Venoms/pharmacology ; Humans ; Reactive Oxygen Species/metabolism
    Chemical Substances Antimicrobial Cationic Peptides ; Antineoplastic Agents ; Fish Venoms ; Reactive Oxygen Species ; pardaxin (67995-63-5) ; Caspase 3 (EC 3.4.22.-) ; Caspase 7 (EC 3.4.22.-)
    Language English
    Publishing date 2011-10-19
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2175190-0
    ISSN 1660-3397 ; 1660-3397
    ISSN (online) 1660-3397
    ISSN 1660-3397
    DOI 10.3390/md9101995
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Piscidin-1, an antimicrobial peptide from fish (hybrid striped bass morone saxatilis x M. chrysops), induces apoptotic and necrotic activity in HT1080 cells.

    Lin, Heng-Ju / Huang, Tsui-Chin / Muthusamy, Sasikala / Lee, Jheng-Fong / Duann, Yeh-Fang / Lin, Cheng-Hui

    Zoological science

    2012  Volume 29, Issue 5, Page(s) 327–332

    Abstract: Piscidin-1, a 22-residue cationic peptide isolated from mast cells of a hybrid striped bass, has potent antimicrobial activities against both gram-positive and -negative bacteria. To date, there is no report of its antitumor activity on any tumor cell ... ...

    Abstract Piscidin-1, a 22-residue cationic peptide isolated from mast cells of a hybrid striped bass, has potent antimicrobial activities against both gram-positive and -negative bacteria. To date, there is no report of its antitumor activity on any tumor cell lines. In this study, we examined the antitumor activity of a synthetic piscidin-1 peptide against several human cancer cell lines using an MTS assay and soft-agar colony-formation assay. We found that a low dose of piscidin induces both apoptosis and necrosis in HT1080 cells, as shown by annexin-V/propidium iodide and acridine orange/ethidium bromide staining, and triggers a necrotic cell death pathway in a short period with high-dose treatment. The destruction of cell membranes by piscidin-1 was demonstrated by transmission electron microscopy. Furthermore, piscidin-1 also inhibits the migration of HT1080 cells in a dose-dependent manner. This study provides the first evidence of the anticancer activity of the antimicrobial peptide, piscidin-1, with potential implications for the treatment of cancer.
    MeSH term(s) Animals ; Antimicrobial Cationic Peptides/genetics ; Antimicrobial Cationic Peptides/metabolism ; Antimicrobial Cationic Peptides/pharmacology ; Antineoplastic Agents/metabolism ; Antineoplastic Agents/pharmacology ; Bass/genetics ; Bass/metabolism ; Cell Line, Tumor ; Fish Proteins/genetics ; Fish Proteins/metabolism ; Fish Proteins/pharmacology ; Gene Expression Regulation ; Humans ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction
    Chemical Substances Antimicrobial Cationic Peptides ; Antineoplastic Agents ; Fish Proteins ; moronecidin protein, Morone saxatilis
    Language English
    Publishing date 2012-05
    Publishing country Japan
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2038883-4
    ISSN 0289-0003
    ISSN 0289-0003
    DOI 10.2108/zsj.29.327
    Database MEDical Literature Analysis and Retrieval System OnLINE

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