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KMID : 0545119960060060445
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 6 p.445 ~ p.450
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Pyridoxatin, an Inhibitor of Gelatinase A with Cytotoxic Activity
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LEE, HO-JAE
CHUNG, MYUNG-CHUL/LEE, CHOONG-HWAN/CHUN, HYO-KON/KIM, HWAN-MOOK/KHO, YUNG-HEE
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Abstract
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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 MIC-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. Pyridocatin is not a peptide analog and has cyclic hydroxamic acid moiety. It inhibited activated gelatinase A with an IC_50 value of 15.2 ??M 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 IC_50 value of 2.92 ??M in PC-3 prostate cancer cells by [^3H] thymidine incorporation assay.
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