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Blood, 15 August 2000, Vol. 96, No. 4, pp. 1490-1495
IMMUNOBIOLOGY
Histone deacetylase inhibitors suppress IL-2-mediated
gene expression prior to induction of apoptosis
Yuko Koyama,
Masaaki Adachi,
Masuo Sekiya,
Mutsuhiro Takekawa, and
Kohzoh Imai
From the First Department of Internal Medicine,
Sapporo Medical University School of Medicine, Sapporo,
Japan.
Histone deacetylase (HDAC) inhibitors can induce transcriptional
activation of a number of genes and induce cellular differentiation as
histone acetylation levels increase. Although these inhibitors induce
apoptosis in several cell lines, the precise mechanism by which they do
so remains obscure. This study shows that HDAC inhibitors, sodium
butyrate and trichostatin A (TSA), abrogate interleukin
(IL)-2-mediated gene expression in IL-2-dependent cells. The HDAC
inhibitors readily induced apoptosis in IL-2-dependent ILT-Mat cells
and BAF-B03 transfectants expressing the IL-2 receptor  c chain,
whereas they induced far less apoptosis in cytokine-independent K562
cells. However, these inhibitors similarly increased acetylation levels
of histones in both cells. Although histone hyperacetylation is
believed to lead to transcriptional activation, the results showed an
abrogation of IL-2-mediated induction of c-myc,
bag-1, and LC-PTP gene expression. This
observed abrogation of gene expression occurred prior to
phosphatidylserine externalization, a process that occurs in early
apoptotic cells. Considering the biologic role played by
IL-2-mediated gene expression in cell survival, these data suggest
that its abrogation may contribute to the apoptotic process induced by
HDAC inhibitors.
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