한빛사 논문
Abstract
Joong Sup Shim1, Jin Hee Kim1, Hyun Young Cho2, Young Na Yum2, Seung Hee Kim2, Hyun-Ju Park3, Bum Sang Shim4, Seung Hoon Choi4, and Ho Jeong Kwon1*
1Department of Bioscience and Biotechnology, Institute of Bioscience, Sejong University, Seoul 143-747 2National Institute of Toxicological Research, Korea Food and Drug Administration, Seoul 122-704 3College of Pharmacy, Sungkyunkwan University, Suwon 440-746 4College of Oriental Medicine, Kyung Hee University, Seoul 130-701, Korea
ABSTRACT
CD13/aminopeptidase N (APN) is a membrane-bound, zinc-dependent metalloproteinase that plays a key role in tumor invasion and angiogenesis. Here, we show that curcumin, a phenolic natural product, binds to APN and irreversibly inhibits its activity. The direct interaction between curcumin with APN was confirmed both in vitro and in vivo by surface plasmon resonance analysis and an APN-specific antibody competition assay, respectively. Moreover, curcumin and other known APN inhibitors strongly inhibited APN-positive tumor cell invasion and basic fibroblast growth factor-induced angiogenesis. However, curcumin did not inhibit the invasion of APN-negative tumor cells, suggesting that the antiinvasive activity of curcumin against tumor cells is attributable to the inhibition of APN. Taken together, our study revealed that curcumin is a novel irreversible inhibitor of APN that binds to curcumin resulting in inhibition of angiogenesis.
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