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Sirtuin 1 is a key regulator of the interleukin-12 p70/interleukin-23 balance in human dendritic cells

AuthorsAlvarez, Yolanda CSIC ORCID; Rodríguez, Mario CSIC ORCID; Municio, Cristina CSIC ORCID; Hugo, Etzel; Alonso, Sara CSIC; Ibarrola, Nieves CSIC ; Fernández, Nieves CSIC ORCID; Sánchez Crespo, Mariano
KeywordsNF-κB (NF-KB)
Histone deacetylase
Dendritic cells
Issue Date2012
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 287(42): 35689-35701 (2012)
AbstractStimulation of human dendritic cells with the fungal surrogate zymosan produces IL-23 and a low amount of IL-12 p70. Trans-repression of il12a transcription, which encodes IL-12 p35 chain, by proteins of the Notch family and lysine deacetylation reactions have been reported as the underlying mechanisms, but a number of questions remain to be addressed. Zymosan produced the location of sirtuin 1 (SIRT1) to the nucleus, enhanced its association with the il12a promoter, increased the nuclear concentration of the SIRT1 co-substrate NAD +, and decreased chromatin accessibility in the nucleosome-1 of il12a, which contains a κB-site. The involvement of deacetylation reactions in the inhibition of il12a transcription was supported by the absence of Ac-Lys-14-histone H3 in dendritic cells treated with zymosan upon coimmunoprecipitation of transducin- like enhancer of split. In contrast, we did not obtain evidence of a possible effect of SIRT1 through the deacetylation of c-Rel, the central element of the NF-κB family involved in il12a regulation. These data indicate that an enhancement of SIRT1 activity in response to phagocytic stimuli may reduce the accessibility of c-Rel to the il12a promoter and its transcriptional activation, thus regulating the IL-12 p70/IL-23 balance and modulating the ongoing immune response. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Identifiersdoi: 10.1074/jbc.M112.391839
issn: 0021-9258
e-issn: 1083-351X
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