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Journal article

Identification of catechols as histone-lysine demethylase inhibitors

By Nielsen, Anders L1; Kristensen, Line H; Stephansen, Karen B; Kristensen, Jan B L; Helgstrand, Charlotte; Lees, Michael; Cloos, Paul; Helin, Kristian; Gajhede, Michael; Olsen, Lars

From

Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.1

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.

Language: English
Year: 2012
Pages: 1190-1194
ISSN: 18733468 and 00145793
Types: Journal article
DOI: 10.1016/j.febslet.2012.03.001
ORCIDs: Helin, Kristian and Gajhede, Michael
Keywords

Catechols Dose-Response Relationship, Drug Enzyme-Linked Immunosorbent Assay Histone Demethylases Histone lysine demethylase Humans Inhibitor Natural product Tumor Cells, Cultured

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