Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Control of histone acetylation is a part of the epigenetic mechanism that regulates gene expression and chromatin architecture. The members of the bromodomain and extra terminal domain (BET) protein family are a group of epigenetic readers that recognize histone acetylation, whereas histone deacetyl- ases such as sirtuin 1 (SIRT1) function as epigenetic erasers. We observed that BET inhibition by the specific inhibitor JQ1 upregulated SIRT1 expression and activated SIRT1. Moreover, we observed that BET inhibition functionally reversed the pro-inflammatory effect of SIRT1 inhibition in a cellular lung disease model. SIRT1 activation is desirable in many age-related, metabolic and inflammatory diseases; our results suggest that BET protein inhibition would be beneficial in treatment of those conditions. Most importantly, our findings demonstrate a novel mechanism of SIRT1 activation by inhibition of the BET proteins.

Original publication




Journal article



Publication Date





1997 - 2001


SIRT1, acetylation, bromodomain and extra terminal domain protein, cancer, epigenetics, gene expression, Animals, Azepines, Cell Line, Cell Line, Tumor, Epigenesis, Genetic, HEK293 Cells, Humans, Inflammation, MCF-7 Cells, Mice, Nuclear Proteins, Protein-Serine-Threonine Kinases, RNA Interference, RNA, Small Interfering, Sirtuin 1, Transcription Factors, Triazoles, Up-Regulation