Pyridoxatin, an inhibitor of gelatinase A with cytotoxic activity

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Pyridoxatin, an inhibitor of gelatinase A with cytotoxic activity
Ho Jae Lee; Myung Chul Chung; Choong Hwan Lee; Hyo Kon Chun; Hwan Mook Kim; Yung Hee Kho
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 6, no. 6, pp. 445-450
Publication Year
Gelatinase A is a member of the matrix metalloproteinases that play an important role in cancer invasion and metastasis. In the course of screening gelatinase A inhibitors from microbial sources, a fungal strain PT-262 showed a strong inhibitory activity. The strain was identified as Chaunopycnis alba on the basis of its morphological characteristics. The inhibitor was isolated from acetone extract of mycelial cake by sequential chromatographies on MCI-gel, Sephadex LH-20, and a reverse-phase HPLC column. The purified inhibitor was identified as pyridoxatin by its physico-chemical properties and spectroscopic analysis. Pyridoxatin is not a peptide analog and has cyclic hydroxamic acid moiety. It inhibited activated gelatinase A with an IC50 value of 15.2 μM using fluorescent synthetic peptide. It also had a strong cytotoxicity against human cancer cell lines in vitro. Furthermore, this compound inhibited DNA synthesis with an IC50 value of 2.92 μM in PC-3 prostate cancer cells by [3H]thymidine incorporation assay.
Chaunopycnis alha PT-262DNA synthesis inhibitorGelatinase A inhibitorcytotoxicityPyridoxatin
Korea Soc-Assoc-Inst
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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