Suppression of caspase-11 expression by histone deacetylase inhibitors

Journal Article · Fri Jan 02 04:00:00 EST 2009 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2008.11.009· OSTI ID:21255819

Heo, Hyejung; Yoo, Lang ^[1]; Shin, Ki Soon ^[2]

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1. Department of Molecular Biology, Sejong University, 98 Gunja-dong, Gwangjin-gu, Seoul 143-747 (Korea, Republic of)
2. Department of Biology and Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701 (Korea, Republic of)

It has been well documented that histone deacetylase inhibitors suppress inflammatory gene expression. Therefore, we investigated whether histone deacetylase inhibitors modulate the expression of caspase-11 that is known as an inducible caspase regulating both inflammation and apoptosis. In the present study, we show that sodium butyrate and trichostatin A, two structurally unrelated inhibitors of histone deacetylase (HDAC), effectively suppressed the induction of caspase-11 in mouse embryonic fibroblasts stimulated with lipopolysaccharides. Sodium butyrate inhibited the activation of upstream signaling events for the caspase-11 induction such as activation of p38 mitogen-activated protein kinase and c-Jun N-terminal kinase, degradation of inhibitor of {kappa}B, and activation of nuclear factor-{kappa}B. These results suggest that the HDAC inhibitor suppressed cytosolic signaling events for the induction of caspase-11 by inhibiting the deacetylation of non-histone proteins.

• OSTI ID: 21255819
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 378; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
APOPTOSIS
CARBOXYLIC ACID SALTS
FIBROBLASTS
GENES
INFLAMMATION
INHIBITION
LIPOPOLYSACCHARIDES
PROTEINS
SODIUM COMPOUNDS