Suppression of inflammation by a synthetic histone mimic

Edwige Nicodeme, Kate L. Jeffrey, Uwe Schaefer, Soren Beinke, Scott Dewell, Chun-wa Chung, Rohit Chandwani, Ivan Marazzi, Paul Wilson, Hervé Coste, Julia White, Jorge Kirilovsky, Charles M. Rice, Jose M. Lora, Rab K. Prinjha, Kevin Lee () and Alexander Tarakhovsky ()
Additional contact information
Edwige Nicodeme: Centre de Recherche GSK
Kate L. Jeffrey: Laboratory of Lymphocyte Signaling, The Rockefeller University
Uwe Schaefer: Laboratory of Lymphocyte Signaling, The Rockefeller University
Soren Beinke: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre
Scott Dewell: Genomics Resource Center, The Rockefeller University
Chun-wa Chung: GlaxoSmithKline R&D, Medicines Research Centre
Rohit Chandwani: Laboratory of Lymphocyte Signaling, The Rockefeller University
Ivan Marazzi: Laboratory of Lymphocyte Signaling, The Rockefeller University
Hervé Coste: Centre de Recherche GSK
Julia White: GlaxoSmithKline R&D, Medicines Research Centre
Jorge Kirilovsky: Centre de Recherche GSK
Charles M. Rice: Laboratory of Virology and Infectious Disease, The Rockefeller University
Jose M. Lora: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre
Rab K. Prinjha: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre
Kevin Lee: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre
Alexander Tarakhovsky: Laboratory of Lymphocyte Signaling, The Rockefeller University

Nature, 2010, vol. 468, issue 7327, 1119-1123

Abstract: Histone mimics target BET bromodomains Small molecules that perturb chromatin proteins are an emerging focus of current biomedical research. Two groups reporting in this issue have targeted bromodomain-containing BET proteins that bind acetylated lysine residues during gene activation, arriving at cell-permeable small molecule compounds with similar structures based on fused triazole-diazepine rings. James Bradner and colleagues report the development of a compound named JQ1. The BET protein BRD4, with two bromodomains, is implicated in human squamous cell carcinoma. JQ1 inhibits the growth of BRD4-dependent tumours in mouse models. Alexander Tarakhovsky and colleagues' inhibitor, I-BET, is shown to interfere with the binding of certain BET family members to acetylated histones. It inhibits activation of pro-inflammatory genes in macrophages and has immunomodulatory activity in a mouse model of inflammatory disease.

Date: 2010
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DOI: 10.1038/nature09589

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