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DNA intercalator korkormicin A preferentially kills tumor cells expressing wild type p53

  1. Author:
    Kitagaki, J.
    Yang, Y. L.

  2. Author Address

    [Kitagaki, J; Yang, YL] NCI, Canc & Dev Biol Lab, NIH, Frederick, MD 21702 USA.;Yang, YL (reprint author), NCI, Canc & Dev Biol Lab, NIH, Bldg 538,Rm 224,1050 Boyles St, Frederick, MD 21702 USA;Yili.Yang@nih.gov
    1. Year: 2011
    2. Date: Oct
  2. Journal: Biochemical and Biophysical Research Communications
    1. 414
    2. 1
    3. Pages: 186-191
  4. Type of Article: Article
  5. ISSN: 0006-291X
  1. Abstract:

    Korkormicin A belongs to a family of nature-produced cyclic depsipeptides. It has potent antitumor activity against both leukemia cell P388 and carcinoma cell M109. To further explore its potential as a cancer therapeutic, the mechanism of its antitumor activity was investigated. We found that korkormicin A can bind to DNA through intercalation. It also induces p53 phosphorylation, which leads to inhibition of p53 degradation and activation of p53-dependent transcription. Furthermore, korkormicin A preferentially induces apoptosis in transformed cells retaining wild type p53. As it has been shown that p53 usually induces apoptosis in transformed cells, but only growth arrest in untransformed cells, these results indicate that korkormicin A is a potential antitumor agent for cancers with wild type p53. Published by Elsevier Inc.

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External Sources

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  2. DOI: 10.1016/j.bbrc.2011.09.054
  3. View record in Web of Science®
  4. WOS: 000296215200034

Library Notes

  1. Fiscal Year: FY2011-2012
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