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[Cancer Research 60, 238-241, January 15, 2000]
© 2000 American Association for Cancer Research

Advances in Brief

Nickel Compounds Are Novel Inhibitors of Histone H4 Acetylation1

Limor Broday, Wu Peng, Min-Hao Kuo, Konstantin Salnikow, Maria Zoroddu and Max Costa2

Department of Environmental Medicine [L. B., W. P., K. S., M. C.] and Kaplan Comprehensive Cancer Center [K. S., M. C.], New York University School of Medicine, New York, New York 10016; Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824-1319 [M-H. K.]; and University of Sassari, 07100 Sassari, Italy [M. Z.]

Environmental factors influence carcinogenesis by interfering with a variety of cellular targets. Carcinogenic nickel compounds, although generally inactive in most gene mutation assays, induce chromosomal damage in heterochromatic regions and cause silencing of reporter genes when they are located near telomere or heterochromatin in either yeast or mammalian cells. We studied the effects of nickel on the lysine acetylation status of the NH2-terminal region of histone H4. At nontoxic levels, nickel decreased the levels of histone H4 acetylation in vivo in both yeast and mammalian cells, affecting only lysine 12 in mammalian cells and all of the four lysine residues in yeast. In yeast, lysine 12 and 16 were more greatly affected than lysine 5 and 8. Interestingly, a histidine Ni2+ anchoring site is found at position 18 from the NH2-terminal tail of H4. Nickel was also found to inhibit the acetylation of H4 in vitro using purified recombinant histone acetyltransferase. To our knowledge, this is the first agent shown to decrease histone H4 acetylation at nontoxic levels.




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