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The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells

  • Authors:
    • Lijie Xia
    • Yanling Wu
    • Ji Ma
    • Jianhua Yang
    • Fuchun Zhang
  • View Affiliations / Copyright

    Affiliations: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, Xinjiang 830046, P.R. China, Department of Pediatrics, Texas Children's Cancer Center, Dan L. Duncan Cancer Center, Baylor College of Medicine, Texas, TX 77030, USA
    Copyright: © Xia et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
  • Pages: 57-62
    |
    Published online on: May 17, 2016
       https://doi.org/10.3892/ol.2016.4601
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Abstract

CecropinXJ is a cationic antimicrobial peptide originally isolated from the larvae of Bombyx mori. The anticancer effect of cecropinXJ has been reported in various tumor cells, including leukemia, gastric and esophageal cancer cells. However, the activity of cecropinXJ on hepatocellular carcinoma (HCC) and its underlying mechanism have not been investigated to date. Therefore, the present study investigated the efficacy and associated mechanism of cecropinXJ in Huh‑7 cells. Flow cytometric analysis was performed to determine the presence of cell cycle arrested and apoptotic cells. CecropinXJ significantly inhibited the growth of Huh‑7 cells in a dose‑ and time‑dependent manner. CecropinXJ treatment for 24 h induced S cell cycle arrest and apoptosis, in addition to loss of the mitochondrial membrane potential, in hepatoma cells. CecropinXJ induced HCC cell apoptosis by activating caspase-3 and poly(ADP-ribose) polymerase. Furthermore, cecropinXJ downregulated the expression of B‑cell lymphoma 2 (Bcl‑2), while upregulated the expression of Bcl‑2‑associated death promoter and Bcl‑2‑associated X protein. In conclusion, the results of the present study suggest that cecropinXJ may be an active anti-HCC agent and provide novel insights into the mechanism of cecropinXJ.
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Copy and paste a formatted citation
Spandidos Publications style
Xia L, Wu Y, Ma J, Yang J and Zhang F: The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells. Oncol Lett 12: 57-62, 2016.
APA
Xia, L., Wu, Y., Ma, J., Yang, J., & Zhang, F. (2016). The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells. Oncology Letters, 12, 57-62. https://doi.org/10.3892/ol.2016.4601
MLA
Xia, L., Wu, Y., Ma, J., Yang, J., Zhang, F."The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells". Oncology Letters 12.1 (2016): 57-62.
Chicago
Xia, L., Wu, Y., Ma, J., Yang, J., Zhang, F."The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells". Oncology Letters 12, no. 1 (2016): 57-62. https://doi.org/10.3892/ol.2016.4601
Copy and paste a formatted citation
x
Spandidos Publications style
Xia L, Wu Y, Ma J, Yang J and Zhang F: The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells. Oncol Lett 12: 57-62, 2016.
APA
Xia, L., Wu, Y., Ma, J., Yang, J., & Zhang, F. (2016). The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells. Oncology Letters, 12, 57-62. https://doi.org/10.3892/ol.2016.4601
MLA
Xia, L., Wu, Y., Ma, J., Yang, J., Zhang, F."The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells". Oncology Letters 12.1 (2016): 57-62.
Chicago
Xia, L., Wu, Y., Ma, J., Yang, J., Zhang, F."The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells". Oncology Letters 12, no. 1 (2016): 57-62. https://doi.org/10.3892/ol.2016.4601
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