Cited by 343Histone Deacetylase Inhibitors ResearchImmune Response and InflammationGenomics and Chromatin Dynamics

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Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection

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Roger, Thierry, Lugrin, Jérôme, Le Roy, Didier, Goy, Geneviève, Mombelli, Matteo, Koessler, Thibaud, Ding, Xavier C., Chanson, Anne-Laure, Reymond, Marlies Knaup, Miconnet, Isabelle, Schrenzel, Jacques, François, Patrice, Calandra, Thierry·2011·Blood

DOI 10.1182/blood-2010-05-284711

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Abstract

Regulated by histone acetyltransferases and deacetylases (HDACs), histone acetylation is a key epigenetic mechanism controlling chromatin structure, DNA accessibility, and gene expression. HDAC inhibitors induce growth arrest, differentiation, and apoptosis of tumor cells and are used as anticancer agents. Here we describe the effects of HDAC inhibitors on microbial sensing by macrophages and dendritic cells in vitro and host defenses against infection in vivo. HDAC inhibitors down-regulated the expression of numerous host defense genes, including pattern recognition receptors, kinases, transcription regulators, cytokines, chemokines, growth factors, and costimulatory molecules as assessed by genome-wide microarray analyses or innate immune responses of macrophages and dendritic cells stimulated with Toll-like receptor agonists. HDAC inhibitors induced the expression of Mi-2β and enhanced the DNA-binding activity of the Mi-2/NuRD complex that acts as a transcriptional repressor of macrophage cytokine production. In vivo, HDAC inhibitors increased the susceptibility to bacterial and fungal infections but conferred protection against toxic and septic shock. Thus, these data identify an essential role for HDAC inhibitors in the regulation of the expression of innate immune genes and host defenses against microbial pathogens.

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Delaloye, J., Roger, T., Steiner, Q., Roy, D. L., Reymond, M. K., Akira, S., Pétrilli, V., Gómez, C. E., Perdiguero, B., Tschopp, J., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000480 · Cited by 307
Self-citation
Retracted
IL-17 and th17 cells
Korn, T., Bettelli, E., Oukka, M., & Kuchroo, V. K. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132710 · Cited by 4,873
Interleukin-12 and the regulation of innate resistance and adaptive immunity
Trinchieri, G. (2003) · Nature reviews. Immunology · doi:10.1038/nri1001 · Cited by 4,007
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Recognition of microorganisms and activation of the immune response
Medzhitov, R. (2007) · Nature · doi:10.1038/nature06246 · Cited by 2,862
The many roles of histone deacetylases in development and physiology: implications for disease and therapy
Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
Macrophage migration inhibitory factor: a regulator of innate immunity
Calandra, T., & Roger, T. (2003) · Nature reviews. Immunology · doi:10.1038/nri1200 · Cited by 1,782
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Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542
Extracellular histones are major mediators of death in sepsis
Xu, J., Zhang, X., Pelayo, R., Monestier, M., Ammollo, C. T., Semeraro, F., Taylor, F. B., Esmon, N. L., Lupu, F., & Esmon, C. T. (2009) · Nature Medicine · doi:10.1038/nm.2053 · Cited by 1,540

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Authors: Roger, T., Lugrin, J., Le Roy, D., Goy, G., Mombelli, M., Koessler, T., Ding, X. C., Chanson, A.-L., Reymond, M. K., Miconnet, I., Schrenzel, J., François, P., & Calandra, T.
Affiliations: Centre Hospitalier Universitaire Vaudois (CH)
Infectious Diseases Service, Department of Medicine, Centre Hospitalier Universitaire Vaudois and University of Lausanne, Lausanne, Switzerland;
University Hospital of Geneva (CH)
ORCID: Roger, Thierry
Lugrin, Jérôme
Mombelli, Matteo
Koessler, Thibaud
Ding, Xavier C.
Schrenzel, Jacques
François, Patrice
Calandra, Thierry
Venue: Blood
Publisher: American Society of Hematology
Published: 2011-01-27
Volume: 117
Issue: 4
Pages: 1205-1217
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood-2010-05-284711
OpenAlex: W2066887945
Cited by: 341
References: 51
Citations by year: 2026: 8 · 2025: 11 · 2024: 13 · 2023: 17 · 2022: 23 · 2021: 23 · 2020: 26 · 2019: 18 · 2018: 24 · 2017: 23 · 2016: 38 · 2015: 23 · 2014: 28 · 2013: 28 · 2012: 24
FWCI: 8.59
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
PubMed (publishedVersion)
Archive ouverte UNIGE (University of Geneva) (publishedVersion)
IRIS (submittedVersion)
SERVAL (Université de Lausanne) (submittedVersion)
Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: histone deacetylase inhibitors, innate immunity, TLR agonists, macrophages, dendritic cells, histone acetylation, epigenetic regulation, NuRD complex, host defense genes, cytokine production, bacterial infection susceptibility, fungal infection susceptibility, septic shock, pattern recognition receptors
MeSH terms: Animals, Cells, Cultured, Disease Models, Animal, Drug Evaluation, Preclinical, Female, Gene Expression Regulation, Humans, Immunity, Innate, Infections, Macrophages, Mice, Inbred BALB C, Down-Regulation, Gene Expression Profiling, Microarray Analysis, Toll-Like Receptors, Mice, Histone Deacetylase Inhibitors

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Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection

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