Corrective socialization in foster care of children

Christensen, Glen; Fine, Paul

doi:10.1007/bf01433634

Cited by 6 publications

(1 citation statement)

References 11 publications

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“…The levels of HDAC1 mRNA, protein and enzyme activity increased when resting lymphocytes were growth-stimulated by interleukin-2 (IL-2). Several biological processes like spherulation of the slime mold Physarum polycephalum [22], and spermatogenesis in rat [23], trout [24], rooster [25] and Drosophila [26] are accompanied by changes in histone acetylation levels. Furthermore, studies in P. polycephalum revealed cell cycle speci¢c di¡erences in the acetylation patterns of core histones [27,28].…”

Section: Introductionmentioning

confidence: 99%

Histone H4 acetylation during interleukin‐2 stimulation of mouse T cells

et al. 1998

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Proliferation and cell cycle progression of eukaryotic cells are closely linked to changes in chromatin structure and gene expression. By reversible histone acetylation the cell is able to modulate chromatin condensation and accessibility of specific regions within the chromatin. Here, we examined histone H4 acetylation patterns during growth induction of the murine interleukin-2 dependent T cell line B6.1. In order to detect acetylation on each of the four potential target residues we produced a set of antibodies recognizing specifically acetylated lysine 5, 8, 12 and 16 in the N-terminal tail of histone H4. Acetylation was generally low in resting T cells, but increased after stimulation with a specific kinetics for each lysine. Lysine 16 was acetylated during the G1 phase and deacetylated during S phase. H4 acetylation on lysine 5, 8 and 12, in contrast, was induced before cells started to replicate, and persisted until cells entered mitosis. Treatment of resting B6.1 cells with the specific deacetylase inhibitor trichostatin A (TSA) led to H4 hyperacetylation at all four lysine residues indicating that the histone modification can occur in the absence of replication. After release from TSA treatment normal H4 acetylation levels were reestablished by extremely rapid deacetylation of lysines 5, 8, 12 and 16. The deacetylation step was 60^100 times faster than TSA induced acetylation and equally efficient in resting and exponentially growing T cells. Our results indicate the presence of cell cycle regulated lysine specific acetylating and deacetylating activities in mouse T cells.z 1998 Federation of European Biochemical Societies.

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