title: Induction of histone acetylation in mouse erythroleukemia cells by some organosulfur compounds including allyl isothiocyanate.
abstract: In previous studies we observed that some allyl sulfides can cause increased acetylation of histones and differentiation in DS19 mouse erythroleukemia cells. In the present work we observed increased acetylation of histones with allyl isothiocyanate and butanethiol but not with butyl sulfide or butyl disulfide. Increased acetylation of histones was established by change in electrophoretic mobility, incorporation of [3H]acetate or immunoblotting. Histone deacetylase in nuclei of DS19 cells was inhibited 74% by 0.5 mM allyl mercaptan and 43% by 0.5 mM butanethiol but was not significantly affected by 0.5 mM allyl isothiocyanate. There was some degree of reversibility in the effect of allyl isothiocyanate when the cells were incubated for 15 hr in fresh medium. The data suggested that allyl isothiocyanate may stimulate histone acetylation rather than inhibit histone deacetylation. Addition of allyl isothiocyanate, however, had very little or no additional effect on the induction of histone acetylation caused by trichostatin A. Histone acetyltransferase activity determined in cell homogenates was not increased by preincubation of cells with allyl isothiocyanate or inclusion of allyl isothiocyanate in the assay medium. It was concluded that treatment of mouse erythroleukemia cells with allyl isothiocyanate can cause increased acetylation of histones but the mechanism for this effect requires further elucidation.
authors.affiliation: Department of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School, Newark, NJ 07103, USA. lea@umdnj.edu
authors.forename: M A
authors.initials: MA
authors.lastname: Lea
authors.forename: V M
authors.initials: VM
authors.lastname: Randolph
authors.forename: J E
authors.initials: JE
authors.lastname: Lee
authors.forename: C
authors.initials: C
authors.lastname: desBordes
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000498:Allyl Compounds / Q000494:pharmacology*; D000818:Animals; D001560:Benzidines / Q000494:pharmacology; D002467:Cell Nucleus / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006454:Hemoglobins / Q000378:metabolism; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology; D015151:Immunoblotting; D017879:Isothiocyanates / Q000494:pharmacology*; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism*; D051379:Mice; D029701:Saccharomyces cerevisiae Proteins; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D013997:Time Factors; D014407:Tumor Cells, Cultured
chemical_list: D000498:Allyl Compounds; D001560:Benzidines; D004791:Enzyme Inhibitors; D006454:Hemoglobins; D006657:Histones; D006877:Hydroxamic Acids; D017879:Isothiocyanates; D029701:Saccharomyces cerevisiae Proteins; D013438:Sulfhydryl Compounds; C029876:benzidine; C037152:isothiocyanic acid; C012589:trichostatin A; C025540:n-butyl mercaptan; C004471:allyl isothiocyanate; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases