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Cell differentiation along multiple pathways accompanied by changes in histone acetylation status

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Post-translational modification of histones is fundamental to the regulation of basic nuclear processes and subsequent cellular events, including differentiation. In this study, we analyzed acetylated forms of histones H2A, H2B, and H4 during induced differentiation in mouse (mESCs) and human (hESCs) embryonic stem cells and during induced enterocytic differentiation of colon cancer cells in vitro. Endoderm-like differentiation of mESCs induced by retinoic acid and enterocytic differentiation induced by histone deacetylase inhibitor sodium butyrate were accompanied by increased mono-, di-, and tri-acetylation of histone H2B and a pronounced increase in di- and tri-acetylation of histone H4. In enterocytes, mono-acetylation of histone H2A also increased and tetra-acetylation of histone H4 appeared only after induction of this differentiation pathway. During differentiation of hESCs, we observed increased mono-acetylation and decreased tri-acetylation of H2B. Mono-, di-, and tri-acetylation of H4 were reduced, manifested by a significant increase in nonacetylated H4 histones. Levels of acetylated histones increased during induced differentiation in mESCs and during histone deacetylase (HDAC) inhibitor-induced enterocytic differentiation, whereas differentiation of human ESCs was associated with reduced acetylation of histones H2B and H4.
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Keywords: MALDI-TOF; acetylation; chromatin; chromatine; epigenetics; histones; l’acétylation; l’épigénétique

Document Type: Research Article

Affiliations: 1: Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Královopolská 135, 612 65 Brno, Czech Republic. 2: Research Group – Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 753/5 Brno, Czech Republic. 3: Institut de Chimie, Université de Nice Sophia Antipolis-UMR CNRS 7272, Parc Valrose, 06100 Nice, France.

Publication date: January 1, 2014

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