Proteomic profiling reveals that collismycin A is an iron chelator

Makoto Kawatani, Makoto Muroi, Akira Wada, Gyo Inoue, Yushi Futamura, Harumi Aono, Kenshirou Shimizu, Takeshi Shimizu, Yasuhiro Igarashi, Naoko Takahashi-Ando, Hiroyuki Osada*


研究成果: Article査読

22 被引用数 (Scopus)


Collismycin A (CMA), a microbial product, has anti-proliferative activity against cancer cells, but the mechanism of its action remains unknown. Here, we report the identification of the molecular target of CMA by ChemProteoBase, a proteome-based approach for drug target identification. ChemProteoBase profiling showed that CMA is closely clustered with di-2-pyridylketone 4,4-dimethyl-3-thiosemicarbazone, an iron chelator. CMA bound to both Fe(II) and Fe(III) ions and formed a 2:1 chelator-iron complex with a redox-inactive center. CMA-induced cell growth inhibition was completely canceled by Fe(II) and Fe(III) ions, but not by other metal ions such as Zn(II) or Cu(II). Proteomic and transcriptomic analyses showed that CMA affects the glycolytic pathway due to the accumulation of HIF-1α. These results suggest that CMA acts as a specific iron chelator, leading to the inhibition of cancer cell growth.

ジャーナルScientific reports
出版ステータスPublished - 2016 12月 6

ASJC Scopus subject areas

  • 一般


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