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Updated: Jul 7, 2026
Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
Published on: November 30, 2018
[Experiment study of PHI on histone methylation and acetylation in Molt-4 cells]
Yi-Qun Huang1, Xu-Dong Ma, Rui-Ji Zhen
1Department of Hematology, Zhangzhou Municipal Hospital, Fujian Medical University, Zhangzhou 363000, China.
Objective:
To investigate the effect of phenyl-hexyl isothiocyanate (PHI) on acetylation and methylation of histone in acute lymphoblastic leukemia cell line Molt4.
Methods:
The inhibition of cell proliferation was observed by MTT method and clone suppression test. Apoptosis and cell cycle arrest were measured by flow cytometry. The alterations in histone acetyltransferase and acetylation and methylation of histones were detected by Western blot.
Results:
PHI could up-regulate the expression of acetyltransferase (P300/CBP), markedly induced the accumulation of acetylated histone H3, H4 and methylated histone H3 lysine 4 (H3K4), and inhibited methylation on lysine 9 of H3 (H3K9). The epigenetic regulation resulted in cell cycle arrest at G0/G1 phase, and induction of apoptosis.
Conclusions:
PHI can modulate both histone methylation and acetylation. It may serve as a histone deacetylase inhibitor, and might be a potential novel anti-leukemia agent.
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