Histone acetylation induced by granulocyte colony-stimulating factor in a map kinase-dependent manner

Y Miyata, M Towatari, Takahiro Maeda, Y Ozawa, Hidehiko Saito

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)655-60
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume283
Issue number3
DOIs
Publication statusPublished - May 11 2001

Fingerprint Dive into the research topics of 'Histone acetylation induced by granulocyte colony-stimulating factor in a map kinase-dependent manner'. Together they form a unique fingerprint.

Cite this