A Protein Phosphatase Is Involved in the Inhibition of Histone Deacetylation by Sodium Butyrate

Cuisset, Laurence; Tichonicky, Lydie; Delpech, Marc

doi:10.1006/bbrc.1998.8698

Cited by 40 publications

(24 citation statements)

References 34 publications

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“…In general, histone acetylation is associated with activation of transcription, whereas histone deacetylation is associated with repression of transcription. Several compounds function as HDAC inhibitors even at a low potency, the result being an accumulation of acetylated histones and an increase in transcriptionally active chromatin (Yoshida et al, 1990;Nakano et al, 1997;Archer et al, 1998;Cuisset et al, 1998;Finnin et al, 1999). Some classes of HDAC inhibitors are under clinical development and these have anticancer effects on a variety of cancer cells.…”

Section: Furthermore Treatment With a Suboptimal Dose Ofintroductionmentioning

confidence: 99%

FR901228 induces tumor regression associated with induction of Fas ligand and activation of Fas signaling in human osteosarcoma cells

et al. 2003

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We investigated the antitumor effects of FR901228, a HDAC inhibitor, on human osteosarcoma cells, in vitro and in vivo to explore its possible utility in the treatment of pediatric bone cancers. FR901228 caused marked growth inhibition with a 50% inhibitory concentration of 1.2-7.3 nM and induction of apoptosis in all eight osteosarcoma cell lines tested. These effects of FR901228 were also observed in vivo xenograft models on BALB/c nude mice, and treatment with 5.6 mg/kg/day resulting in a >70% reduction in the mean final tumor volume compared with the mean initial tumor volume. TUNEL assays demonstrated extensive apoptosis in tumor sections of mice treated with FR901228. Induction of apoptosis was preceded by increased expression of Fas ligand (FasL) mRNA, resulting in expression of membrane-bound FasL, which was followed by sequential activation of caspase-8 and -3. The level of apoptosis induction was reduced using a neutralizing anti-FasL antibody and overexpression of either the dominantnegative FADD or the viral FLICE inhibitory protein.Furthermore, treatment with a suboptimal dose of FR901228 greatly sensitized osteosarcoma cells to agonistic anti-Fas antibody-mediated apoptosis. These findings suggest that FR901228 is a highly promising antitumor agent against osteosarcoma, inducing apoptosis by the activation of the Fas/FasL system.

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Section: Furthermore Treatment With a Suboptimal Dose Ofintroductionmentioning

confidence: 99%

FR901228 induces tumor regression associated with induction of Fas ligand and activation of Fas signaling in human osteosarcoma cells

et al. 2003

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“…Because no changes were noted in the histone acetylation status of the P450arom promoters I.3/II in MCM-stimulated cells in the presence or absence of NaBu, this is not a likely mechanism. The effects of NaBu on a number of cellular functions have been reported previously to be reversed by various kinase or phosphatase inhibitors (31,(53)(54)(55). For example, NaBu treatment was reported to give rise to activation of a type 1 protein phosphatase (31,55).…”

Section: Discussionmentioning

confidence: 96%

A Novel Role of Sodium Butyrate in the Regulation of Cancer-associated Aromatase Promoters I.3 and II by Disrupting a Transcriptional Complex in Breast Adipose Fibroblasts

Deb¹,

Zhou²,

Amin

et al. 2006

Journal of Biological Chemistry

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“…However, the molecular process used to achieve such a regulation still remains undetermined. Histone acetylation is a dynamic process leading to structural changes in the nucleosome particle and strongly associated with transcriptional activity (35)(36)(37). The model to explain the link between transcriptional activity and histone acetylation proposes that this core histone covalent modification would facilitate the access of specific regulatory factors to DNA.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, some of these regulatory factors could act as enzymes that acetylate histones (38)(39)(40). Cuisset et al (35) suggest that a serine-threonine protein phosphatase activity is essential to mediate the effects of sodium butyrate on both gene expression and core histone acetylation in HTC cells. Histone hyperacetylation is then a probable mechanism involved in butyrate-induced apoptosis.…”

Section: Discussionmentioning

confidence: 99%

Butyrate induces apoptosis in murine macrophages via caspase-3, but independent of autocrine synthesis of tumor necrosis factor and nitric oxide

Ramos

Rabelo

Duarte

et al. 2002

Braz J Med Biol Res

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We demonstrated that 4 mM butyrate induces apoptosis in murine peritoneal macrophages in a dose-and time-dependent manner as indicated by studies of cell viability, flow cytometric analysis of annexin-V binding, DNA ladder pattern and the determination of hypodiploid DNA content. The activity of caspase-3 was enhanced during macrophage apoptosis induced by butyrate and the caspase inhibitor z-VAD-FMK (100 µM) inhibited the butyrate effect, indicating the major role of the caspase cascade in the process. The levels of butyrate-induced apoptosis in macrophages were enhanced by cotreatment with 1 µg/ml bacterial lipopolysaccharide (LPS). However, our data indicate that apoptosis induced by butyrate and LPS involves different mechanisms. Thus, LPS-induced apoptosis was only observed when macrophages were primed with IFN-γ and was partially dependent on iNOS, TNFR1 and IRF-1 functions as determined in experiments employing macrophages from various knockout mice. In contrast, butyrate-induced macrophage apoptosis was highly independent of IFN-γ priming and of iNOS, TNFR1 and IRF-1 functions. Correspondence

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A Protein Phosphatase Is Involved in the Inhibition of Histone Deacetylation by Sodium Butyrate

Cited by 40 publications

References 34 publications

FR901228 induces tumor regression associated with induction of Fas ligand and activation of Fas signaling in human osteosarcoma cells

FR901228 induces tumor regression associated with induction of Fas ligand and activation of Fas signaling in human osteosarcoma cells

A Novel Role of Sodium Butyrate in the Regulation of Cancer-associated Aromatase Promoters I.3 and II by Disrupting a Transcriptional Complex in Breast Adipose Fibroblasts

Butyrate induces apoptosis in murine macrophages via caspase-3, but independent of autocrine synthesis of tumor necrosis factor and nitric oxide

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