ArticleChembiochem : a European journal of chemical biology2015
BET Inhibition Upregulates SIRT1 and Alleviates Inflammatory Responses.
Article in Chembiochem : a European journal of chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- A randomized study of the safety and pharmacokinetics of GSK3358699, a mononuclear myeloid-targeted bromodomain and extra-terminal domain inhibitor.British journal of clinical pharmacology · 2022Trial
- Article
- Current Trends in Sirtuin Activator and Inhibitor Development.Molecules (Basel, Switzerland) · 2024Review
- Article
- BRD4 inhibition alleviates mechanical stress-induced TMJ OA-like pathological changes and attenuates TREM1-mediated inflammatory response.Clinical epigenetics · 2021Article
- Dissecting pharmacological effects of chloroquine in cancer treatment: interference with inflammatory signaling pathways.Immunology · 2020Review
- Article
- BRD4 Inhibition Protects Against Acute Pancreatitis Through Restoring Impaired Autophagic Flux.Frontiers in pharmacology · 2020Article
- Review
- A Novel Epi-drug Therapy Based on the Suppression of BET Family Epigenetic Readers.The Yale journal of biology and medicine · 2017Review
- Epigenetic polypharmacology: from combination therapy to multitargeted drugs.Clinical epigeneticsReview
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
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.
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Registered trials
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