Histone deacetylase inhibitors, N-butyric acid and trichostatin A, induce caspase-8- but not caspase-9-dependent apoptosis in human malignant glioma cells

Komata, Tadashi; Kanzawa, Takao; Nashimoto, Takeo; Aoki, Hiroshi; Endo, Shunro; Kon, Takashi; Takahashi, Hideo; Kondō, Shōichi; Tanaka, Ryo

doi:10.3892/ijo.26.5.1345

Cited by 15 publications

(13 citation statements)

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“…Some studies have established clear roles for the death receptors and caspase-8 in this process [42,43,47,51]. Our study demonstrated that valproic acid and butyrate promote apoptosis in HeLa cervical cancer cells through a caspase-dependent mechanism (Fig.…”

Section: Discussionsupporting

confidence: 61%

Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B

et al. 2006

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Background: In eukaryotic cells, the genomic DNA is packed with histones to form the nucleosome and chromatin structure. Reversible acetylation of the histone tails plays an important role in the control of specific gene expression. Mounting evidence has established that histone deacetylase inhibitors selectively induce cellular differentiation, growth arrest and apoptosis in variety of cancer cells, making them a promising class of anticancer drugs. However, the molecular mechanisms of the anti-cancer effects of these inhibitors have yet to be understood.

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Section: Discussionsupporting

confidence: 61%

Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B

et al. 2006

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“…Histone deacetylase inhibitors, such as N-butyric acid and trichostatin A, have been shown to increase caspase 8 expression and induce apoptosis in human malignant glioma cells (42). This result suggested that acetylation of histones is important for expression of caspase 8.…”

Section: Discussionmentioning

confidence: 56%

Smad7 Protein Induces Interferon Regulatory Factor 1-dependent Transcriptional Activation of Caspase 8 to Restore Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL)-mediated Apoptosis

Kim

et al. 2013

Journal of Biological Chemistry

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Background: Smad7 may have biological roles other than inhibition of TGF-␤ signaling. Results: Smad7 activates caspase 8 expression by recruiting IRF1, thereby inducing TRAIL-mediated apoptosis. Conclusion: Smad7 functions as a transcriptional coactivator of IRF1 to regulate the expression of target genes. Significance: Smad7-inducing reagents can be used as anti-cancer drugs for tumors that have defects in caspase 8 expression.

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“…We found that the HDAC inhibitor VPA and HDAC1 knockdown experiments resulted in an increase of AIF expression, suggesting that HDAC inhibitors could be used to treat tumors with nuclear BNIP3 expression. Indeed, HDAC inhibitors have been shown to induce apoptosis in glioma cells (Komata et al, 2005). Hence, HDAC inhibitors might mediate de-repression of BNIP3 transcriptional activity and provide a novel target for development of treatments for chemotherapy resistant GBM tumors.…”

Section: Discussionmentioning

confidence: 99%

BNIP3 (Bcl-2 19 kDa Interacting Protein) Acts as Transcriptional Repressor of Apoptosis-Inducing Factor Expression Preventing Cell Death in Human Malignant Gliomas

Burton¹,

Eisenstat²,

Gibson³

2009

J. Neurosci.

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The Bcl-2 19 kDa interacting protein (BNIP3) is a pro-cell-death BH3-only member of the Bcl-2 family. We previously found that BNIP3 is localized to the nucleus in the majority of glioblastoma multiforme (GBM) tumors and fails to induce cell death. Herein, we have discovered that nuclear BNIP3 binds to the promoter of the apoptosis-inducing factor (AIF) gene and represses its expression. BNIP3 associates with PTB-associating splicing factor (PSF) and HDAC1 (histone deacetylase 1) contributing to transcriptional repression of the AIF gene. This BNIP3-mediated reduction in AIF expression leads to decreased temozolomide-induced apoptosis in glioma cells. Furthermore, nuclear BNIP3 expression in GBMs correlates with decreased AIF expression. Together, we have discovered a novel transcriptional repression function for BNIP3 causing reduced AIF expression and increased resistance to apoptosis. Thus, nuclear BNIP3 may confer a survival advantage to glioma cells and explain, in part, why BNIP3 is expressed at high levels in solid tumors, especially GBM.

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Histone deacetylase inhibitors, N-butyric acid and trichostatin A, induce caspase-8- but not caspase-9-dependent apoptosis in human malignant glioma cells

Cited by 15 publications

References 0 publications

Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B

Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B

Smad7 Protein Induces Interferon Regulatory Factor 1-dependent Transcriptional Activation of Caspase 8 to Restore Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL)-mediated Apoptosis

BNIP3 (Bcl-2 19 kDa Interacting Protein) Acts as Transcriptional Repressor of Apoptosis-Inducing Factor Expression Preventing Cell Death in Human Malignant Gliomas

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