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Increased Histone Acetylation and Deacetylation in Rat Ascites Hepatoma Cells¹

Departments of Chemistry [K. H., D. F.] and Internal Medicine [K. K.], Hamamatsu University School of Medicine, Hamamatsu 431-31 Japan, and Department of Internal Medicine [M. F.], Aichi Cancer Center, Chikusa-ku, Nagoya 464, Japan

Rates of histone acetylation and deacetylation in nuclei from fetal, adult, and two kinds of neoplastic rat hepatocytes were examined. Histone acetylation in isolated nuclei was measured in the presence of 6 mM sodium n-butyrate, a potent inhibitor of deacetylase, and in the absence of the inhibitor. The deacetylase activity was estimated from the difference between the rates with or without the inhibitor. Both histone acetylation and deacetylation in nuclei from hepatoma cells (AH 66 cells) occurred two times faster than those of nuclei from fetal and adult livers regardless of -fetoprotein production. This increased acetylation and deacetylation in hepatoma cells may be ascribed to either the increased activities of the enzymes or the increased accessibility of histone to the enzymes in the chromatin. Autoradiographic analysis of acetylated histones showed that all of the internal histones of the nucleosomes were acetylated and that no apparent difference was found in the pattern of acetylated fractions between hepatoma nuclei and normal liver cell nuclei.

¹ This research was supported in part by Grants-in-Aid for Scientific Research (468056 and 579155), for Cancer Research, and for Special Project Research from the Ministry of Education, Science, and Culture of Japan.

² To whom requests for reprints should be addressed.

Received 5/ 8/80. Accepted 12/31/80.

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