Miyata Y, Towatari M, Maeda T, Ozawa Y, Saito H
First Department of Internal Medicine, Nagoya University School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya, 466-8550, Japan.
Biochem Biophys Res Commun. 2001 May 11;283(3):655-60. doi: 10.1006/bbrc.2001.4840.
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 chromatin immunoprecipitation. 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 signals via G-CSF may be coupled with histone acetylation during the process of gene expression.
组蛋白乙酰化已被证明会影响染色质结构和基因表达。丝裂原活化蛋白（MAP）激酶途径可被多种细胞因子激活，并在造血细胞的存活、增殖和分化中发挥关键作用。我们聚焦于MAP激酶级联反应的一部分以及粒细胞集落刺激因子（G-CSF）在髓过氧化物酶（MPO）这一关键的髓系分化相关基因的组蛋白乙酰化过程中的作用。染色质免疫沉淀结果显示，G-CSF可导致MPO启动子处的组蛋白H3和H4快速乙酰化。此外，CBP和p300会响应G-CSF被招募至启动子区域。此外，我们还表明，G-CSF诱导的组蛋白快速乙酰化依赖于MAP激酶。这些结果说明了在基因表达过程中，经由G-CSF的髓系分化信号可能如何与组蛋白乙酰化相耦合。
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