Identification of catechols as histone–lysine demethylase inhibitors

Anders L. Nielsen, Line H. Kristensen, Karen Stephansen, Jan B. L. Kristensen, Charlotte Helgstrand, Michael Lees, Paul A. Cloos, Kristian Helin, Michael Gajhede, Lars Olsen

FEBS Letters · 2012 · 42 citations · 20 references

DOIFull text

Open access

Concepts

Abstract

Identification of inhibitors of histone-lysine demethylase (HDM) enzymes is important because of their involvement in the development of cancer. An ELISA-based assay was developed for identification of inhibitors of the HDM KDM4C in a natural products library. Based on one of the hits with affinity in the low μM range (1, a catechol), a subset of structurally related compounds was selected and tested against a panel of HDMs. In this subset, two inhibitors (2 and 10) had comparable affinities towards KDM4C and KDM6A but no effect on PHF8. One inhibitor restored H3K9me3 levels in KDM4C transfected U2-OS cells.

References

20