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Histone Acetylation Induced by Granulocyte Colony-Stimulating Factor in a MAP Kinase-Dependent Manner

https://doi.org/10.1006/bbrc.2001.4840Get rights and content

Abstract

Histone acetylation has been shown to affect chromatin structure and gene expression. The mitogen-activated protein (MAP) kinase pathway is activated by a number of cytokines and plays critical roles in hematopoietic cell survival, proliferation, and differentiation. We focused on the part of the MAP kinase cascade and granulocyte colony-stimulating factor (G-CSF)in histone acetylation at one of the critical myeloid differentiation-associated genes, myeloperoxidase (MPO). G-CSF caused rapid acetylation of histone H3 and H4 at the promoter of MPO as revealed by chromatinimmunoprecipitation. In addition, CBP and p300 were recruited to the promoter in response to G-CSF. Furthermore, we showed that rapid histone acetylation induced by G-CSF is MAP kinase-dependent. These results illustrate how myeloid-differentiating signalsvia G-CSF may be coupled with histone acetylation during the process of gene expression.

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Cited by (26)

  • Alcohol exposure increases the expression of cardiac transcription factors through ERK1/2-mediated histone3 hyperacetylation in H9c2 cells

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    ERK1/2 may also activate several types of HATs, and regulate their enzyme aticactivities [27,28]. In GM-162 M cells, the hyperacetylation of both histone3 and histone4 induced by granulocyte colony-stimulating factor is shown to be through the activation of ERK1/2 pathway [29]. Similarly, the data from this study have demonstrated that alcohol-induced activation of ERK1/2 is associated with increased acetylation of histone3.

  • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-κB and pro-inflammatory gene expression

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    Acetylation of histones has been associated with the transcription of a range of inflammatory mediators including IL-8 [62], eotaxin, IL-1β and GM-CSF [63], MIP-2 [64] and IL-6 [65]. Acetylation can occur specifically at the promoter sites of these genes as shown by chromatin immunoprecipitation (ChIP) assays for IL-8 [66], CYP1A1 [67], myeloperoxidase [68], COX-2 [69] and 15-lox-1 [70] gene promoters, indicating acetylation specificity. Oxidative stress and pro-inflammatory mediators have been suggested to influence histone acetylation and phosphorylation, via a mechanism dependent on the activation of the MAPK pathway [71–73].

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