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Article

Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy

  • Authors:
    • Ying Huang
    • Xihan Li
    • Huizi Sha
    • Lianru Zhang
    • Xinyu Bian
    • Xiao Han
    • Baorui Liu
  • View Affiliations / Copyright

    Affiliations: The Comprehensive Cancer Centre, Nanjing Drum Tower Hospital Clinical College of Nanjing Medical University, Nanjing, Jiangsu, P.R. China, State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, P.R. China, The Comprehensive Cancer Centre of Drum Tower Hospital, Medical School of Nanjing University and Clinical Cancer Institute of Nanjing University, Nanjing, Jiangsu, P.R. China, Key Laboratory of Human Functional Genomics of Jiangsu Province, Jiangsu Diabetes Center, Nanjing Medical University, Nanjing, Jiangsu, P.R. China
  • Pages: 2063-2070
    |
    Published online on: February 10, 2017
       https://doi.org/10.3892/or.2017.5440
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Abstract

KLA (sequence, KLAKLAKKLAKLAK) is a peptide which leads to programmed cell death by disrupting the mitochondrial membrane. However, low penetration in tumors greatly limits its application and efficacy. To develop a KLA-based cancer therapy, KLA-iRGD, a recombinant protein was constructed. It consists of the KLA peptide and iRGD (CRGDKGPDC), a tumor-homing peptide with high penetration into tumor tissue and cells. The conjugated KLA exhibits pro-apoptotic activity to prevent the growth of a tumor once it is inside the cell. Once KLA-iRGD is internalized in cultured tumor cells, via the activation of the receptor neuropilin-1, it spreads extensively throughout the mass of the tumor. The recombinant KLA-iRGD protein showed antitumor activity in vivo in mice and in vitro in tumor cell lines. Repeated treatment with KLA-iRGD greatly prevented tumor growth, resulting in a considerable reduction in tumor volume. According to our data, KLA-iRGD may serve as a potential anticancer agent with limited systemic toxicity and high selectivity for the treatment of MKN45 gastric cancer, which may lead to the enhancement of new targeted anticancer agents.
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Copy and paste a formatted citation
Spandidos Publications style
Huang Y, Li X, Sha H, Zhang L, Bian X, Han X and Liu B: Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy. Oncol Rep 37: 2063-2070, 2017.
APA
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., & Liu, B. (2017). Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy. Oncology Reports, 37, 2063-2070. https://doi.org/10.3892/or.2017.5440
MLA
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., Liu, B."Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy". Oncology Reports 37.4 (2017): 2063-2070.
Chicago
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., Liu, B."Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy". Oncology Reports 37, no. 4 (2017): 2063-2070. https://doi.org/10.3892/or.2017.5440
Copy and paste a formatted citation
x
Spandidos Publications style
Huang Y, Li X, Sha H, Zhang L, Bian X, Han X and Liu B: Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy. Oncol Rep 37: 2063-2070, 2017.
APA
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., & Liu, B. (2017). Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy. Oncology Reports, 37, 2063-2070. https://doi.org/10.3892/or.2017.5440
MLA
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., Liu, B."Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy". Oncology Reports 37.4 (2017): 2063-2070.
Chicago
Huang, Y., Li, X., Sha, H., Zhang, L., Bian, X., Han, X., Liu, B."Tumor-penetrating peptide fused to a pro-apoptotic peptide facilitates effective gastric cancer therapy". Oncology Reports 37, no. 4 (2017): 2063-2070. https://doi.org/10.3892/or.2017.5440
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