Cancer Letters
Volume 203, Issue 2 , Pages 163-169, January 2004

Psammaplin A, a marine natural product, inhibits aminopeptidase N and suppresses angiogenesis in vitro

  • Joong Sup Shim

      Affiliations

    • Department of Bioscience and Biotechnology, Institute of Bioscience, Sejong University, 98 Kunja-dong Kwangjin-gu, Seoul 143-747, South Korea
  • ,
  • Hyi-Seung Lee

      Affiliations

    • Marine Natural Products Laboratory, Korea Ocean Research and Development Institute, Ansan 425-600, South Korea
  • ,
  • Jongheon Shin

      Affiliations

    • Natural Products Research Institute, College of Pharmacy, Seoul National University, Seoul 110-460, South Korea
  • ,
  • Ho Jeong Kwon

      Affiliations

    • Department of Bioscience and Biotechnology, Institute of Bioscience, Sejong University, 98 Kunja-dong Kwangjin-gu, Seoul 143-747, South Korea
    • Corresponding Author InformationCorresponding author. Tel.: +82-2-3408-3640; fax: +82-2-3408-3334

Received 5 March 2003; accepted 19 August 2003.

Abstract 

Psammaplin A (PsA) is a phenolic natural product isolated from a marine sponge, which showed a potent cytotoxicity against several cancer cell lines. In present study, PsA was found to inhibit mammalian aminopeptidase N (APN) that plays a key role in tumor cell invasion and angiogenesis. PsA inhibited the APN activity with an IC50 of 18 μM in a non-competitive manner. Moreover, PsA potently inhibited the proliferation of several cancer and endothelial cells. Interestingly, the anti-proliferative effect of PsA was dependent on the cellular amount of APN expression. Finally, PsA suppressed the invasion and tube formation of endothelial cells stimulated by basic fibroblast growth factor. These data demonstrate that PsA is a new inhibitor of APN and can be developed as a novel anti-angiogenic agent.

Keywords: Psammaplin A, Aminopeptidase N, Chemoinvasion, Angiogenesis

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PII: S0304-3835(03)00686-4

doi:10.1016/j.canlet.2003.08.036

Cancer Letters
Volume 203, Issue 2 , Pages 163-169, January 2004