Lysine-specific demethylase 1 (LSD1) and histone deacetylase 1 (HDAC1) synergistically repress proinflammatory cytokines and classical complement pathway components.

Andreas Janzer, Soyoung Lim, Florian Fronhoffs, Naima Niazy, Reinhard Buettner, Jutta Kirfel

Institute of Pathology, University of Bonn, Sigmund-Freud-Str. 25, 53127 Bonn, Germany.

Biochemical and biophysical research communications 2012 May 18

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Histone modifying enzymes confer epigenetic marks, directing the changes in gene expression required for diverse cellular processes. Lysine-specific demethylase 1 (LSD1) functions as a transcriptional coregulator by demethylating histone H3 on lysine 4 and lysine 9. Analyzing transcriptomes on microarrays, we identified genes which represent inflammatory-related targets of LSD1. We demonstrate a repressive role of LSD1 in proinflammatory cytokine expression such as IL1α, IL1β, IL6 and IL8 and classical complement components. Consistently, LSD1 occupies and regulates the promoter of these genes. In addition, we demonstrate that HDAC1 and LSD1 synergistically regulate these inflammatory-related genes. Our data reveal a novel role for LSD1 in suppressing immune responses. Crown Copyright © 2012. Published by Elsevier Inc. All rights reserved.

Citation

Andreas Janzer, Soyoung Lim, Florian Fronhoffs, Naima Niazy, Reinhard Buettner, Jutta Kirfel. Lysine-specific demethylase 1 (LSD1) and histone deacetylase 1 (HDAC1) synergistically repress proinflammatory cytokines and classical complement pathway components. Biochemical and biophysical research communications. 2012 May 18;421(4):665-70