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

Joong Sup Shim; Hyi Seung Lee; Jongheon Shin; Ho Jeong Kwon

doi:10.1016/j.canlet.2003.08.036

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

Joong Sup Shim, Hyi Seung Lee, Jongheon Shin, Ho Jeong Kwon

Research output: Contribution to journal › Article › peer-review

76 Citations (Scopus)

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.

Original language	English
Pages (from-to)	163-169
Number of pages	7
Journal	Cancer Letters
Volume	203
Issue number	2
DOIs	https://doi.org/10.1016/j.canlet.2003.08.036
Publication status	Published - 2004 Jan

Bibliographical note

Funding Information:
This work was supported by a grant number M102KM010001-03K1301-01911 for the 21C Frontier Functional Proteomics Center from the Ministry of Science and Technology, Republic of Korea and the Brain Korea 21 Project.

All Science Journal Classification (ASJC) codes

Oncology
Cancer Research

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.canlet.2003.08.036

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

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.",

author = "Shim, {Joong Sup} and Lee, {Hyi Seung} and Jongheon Shin and Kwon, {Ho Jeong}",

note = "Funding Information: This work was supported by a grant number M102KM010001-03K1301-01911 for the 21C Frontier Functional Proteomics Center from the Ministry of Science and Technology, Republic of Korea and the Brain Korea 21 Project.",

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AU - Shim, Joong Sup

AU - Lee, Hyi Seung

AU - Shin, Jongheon

AU - Kwon, Ho Jeong

N1 - Funding Information: This work was supported by a grant number M102KM010001-03K1301-01911 for the 21C Frontier Functional Proteomics Center from the Ministry of Science and Technology, Republic of Korea and the Brain Korea 21 Project.

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Y1 - 2004/1

N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

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