Histone Deacetylase Inhibitor Sodium Butyrate Enhances the Cell Killing Effect of Psoralen plus UVA by Attenuating Nucleotide Excision Repair

Toyooka, Tatsushi; Ibuki, Yuko

doi:10.1158/0008-5472.can-08-2546

Cited by 27 publications

(31 citation statements)

References 49 publications

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“…It has been reported that different HDACi sensitize tumor cells towards the killing effect of many anticancer agents (11,(45)(46)(47) and this effect has been attributed to interference with DNA repair pathways (8,11,48) or abrogation of the cell-cycle checkpoints (18)(19)(20). Our results suggest that the accumulation of intracellular ROS-mediated increase in the lesion burden may be the major mechanism by which sodium butyrate enhances the cytotoxicity of MMC-treated cells.…”

Section: Discussionsupporting

confidence: 50%

“…However, we did not detect differences in NER capacity between sodium butyrate-treated and -untreated cells. A previous report found reduced NER rate after sodium butyrate treatment (11). The discrepancy could be due to differences in the experimental design (plasmid host cell reactivation vs. cell-based assay) or the cell types used.…”

Section: Discussionmentioning

confidence: 81%

“…The effect on NHEJ, which is the principal DSB repair pathway in mammals, was attributed to downregulation of Ku70 and Ku86 (10) or to the disruption of critical deacetylation events at the break sites (9). Another study found that sodium butyrate attenuated nucleotide excision repair (NER) and enhanced cellkilling effect of psoralen-induced lesions (11). HDACi induce cell death directly via various other mechanisms such as hyperacetylation of promoters of TRAIL, DR5, FAS, and FASL death receptor pathway members (12,13) or production of proapoptotic reactive oxygen species (ROS) and oxidative injury (14)(15)(16)(17).…”

Section: Introductionmentioning

confidence: 99%

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The Inhibitor of Histone Deacetylases Sodium Butyrate Enhances the Cytotoxicity of Mitomycin C

Gospodinov

Popova

Vassileva

et al. 2012

Molecular Cancer Therapeutics

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The use of histone deacetylase inhibitors has been proposed as a promising approach to increase the cell killing effect of DNA damage-inducing drugs in chemotherapy. However, the molecular mechanism of their action remains understudied. In the present article, we have assessed the effect of the histone deacetylase inhibitor sodium butyrate on the DNA damage response induced by the crosslinking agent mitomycin C. Sodium butyrate increased mitomycin C cytotoxicity, but did not impair the repair pathways required to remove mitomycin C-induced lesions as neither the rate of nucleotide excision repair nor the homologous recombination repair rate were diminished. Sodium butyrate treatment abrogated the S-phase cell-cycle checkpoint in mitomycin C-treated cells and induced the G 2 -M checkpoint. However, sodium butyrate treatment alone resulted in accumulation of reactive oxygen species, double-strand breaks in DNA, and apoptosis. These results imply that the accumulation of reactive oxygen species-mediated increase in DNA lesion burden may be the major mechanism by which sodium butyrate enhances the cytotoxicity of mitomycin C. Mol Cancer Ther; 11(10); 2116-26. Ó2012 AACR.

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Section: Discussionsupporting

confidence: 50%

Section: Discussionmentioning

confidence: 81%

Section: Introductionmentioning

confidence: 99%

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The Inhibitor of Histone Deacetylases Sodium Butyrate Enhances the Cytotoxicity of Mitomycin C

Gospodinov

Popova

Vassileva

et al. 2012

Molecular Cancer Therapeutics

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“…Recent studies using high-resolution mass spectrometry have identified 3,600 lysine acetylation sites in 1,750 proteins, among which are 167 acetylation sites in 72 proteins, including GG-NER proteins DDB1, DDB2, CUL4A, and RAD23A (42). However, it appears that histone deacetylases (HDACs) may play critical roles in regulating GG-NER (43,44), further supporting the conclusion that XPC is the major target for SIRT1's enhancement of GG-NER. Recent studies have shown that loss of XPC inhibits DSB repair (45).…”

Section: Discussionmentioning

confidence: 94%

Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C

Ming

Shea

Guo

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

129

125

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Disruption of the nucleotide excision repair (NER) pathway by mutations can cause xeroderma pigmentosum, a syndrome predisposing affected individuals to development of skin cancer. The xeroderma pigmentosum C (XPC) protein is essential for initiating global genome NER by recognizing the DNA lesion and recruiting downstream factors. Here we show that inhibition of the deacetylase and longevity factor SIRT1 impairs global genome NER through suppressing the transcription of XPC in a SIRT1 deacetylase-dependent manner. SIRT1 enhances XPC expression by reducing AKTdependent nuclear localization of the transcription repressor of XPC. Finally, we show that SIRT1 levels are significantly reduced in human skin tumors from Caucasian patients, a population at highest risk. These findings suggest that SIRT1 acts as a tumor suppressor through its role in DNA repair.ucleotide excision repair (NER) is a versatile DNA repair pathway that eliminates a wide variety of helix-distorting base lesions, including UV radiation-induced cyclobutane pyrimidine dimers (CPD) and (6-4) photoproducts (6-4PPs) (1, 2), as well as bulky adducts induced by numerous chemical compounds. Defects in NER by mutations cause the autosomal recessive xeroderma pigmentosum (XP) and Cockayne syndromes (3-5). XP patients are clinically characterized by cutaneous sensitivity to sunlight exposure and a predisposition to skin cancer. Seven NER-deficient genetic complementation groups of XP (XP-A to -G) have been identified, and all of the corresponding genes have now been cloned (3-5).Mammalian NER consists of two distinct subpathways: global genome NER (GG-NER), which operates throughout the genome, and transcription-coupled NER (TC-NER), which specifically removes lesions on the transcribed DNA strand of active genes. A major difference between these two pathways appears to lie in the strategies for detecting damaged bases. Accumulating evidence indicates that the XP group C (XPC) protein plays an essential role in GG-NER-specific damage recognition (6-8). Although biochemical and genetic analyses have characterized the function of XPC in considerable detail, much remains to be elucidated with regard to its regulation and interaction with other critical cellular pathways.Sirtuin 1 (SIRT1), a mammalian counterpart of the yeast silent information regulator 2 (Sir2) and a proto member of the sirtuin family, is an NAD-dependent longevity-promoting deacetylase. SIRT1 is crucial for cell survival, metabolism, senescence, and stress response in several cell types and tissues (9-13). Both histone and nonhistone targets of SIRT1 have been identified, including FOXO, p53, and PPARγ (10,12,14). SIRT1 has been implicated as an important player in cancer. However, it remains unclear whether SIRT1 serves as a tumor suppressor or a tumor promoter (13-16). SIRT1 expression is relatively higher in many malignancies, including colon, breast, prostate, and skin cancers and leukemia, as compared with their corresponding normal tissues (17)(18)(19)(20)(21)(22). But the specific c...

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“…In line with findings of recent studies demonstrating the efficiency of using the HDACi sodium butyrate and TSA together with PUVA therapy in various cell lines [38] and extending on previous studies conducted in this laboratory using UV A Sens and TSA [39], the concept of using combination treatment involving the Hoechst analogue for the treatment of CTCL was further explored. With the effect of HDACi well established, damage in the form of double-strand breaks from UV A radiation was analysed with γH2AX immunofluorescence assays.…”

Section: Discussionmentioning

confidence: 76%

Combination Phototherapy with a Histone Deacetylase Inhibitor and a Potent DNA-Binding Bibenzimidazole: Effects in Haematological Cell Lines

2012

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Current treatment for cutaneous T-cell lymphoma includes phototherapy, which involves either the use of narrowband ultraviolet B light or UV A in combination with a psoralen photosensitiser. Therapy typically involves administration of the photosensitiser followed by topical exposure to UV A . A different approach is extracorporeal photopheresis, an ex vivo strategy which is used for more advanced stages of disease. Further, histone deacetylase inhibitors are emerging as potent anticancer agents with suberoylanilide hydroxamic acid and depsipeptide, having received FDA approval for the treatment of cutaneous T-cell lymphoma. We have developed UV A Sens, an extremely potent, DNA minor groove-binding UV A sensitizer for potential use in phototherapy. We have previously demonstrated the extreme photopotency of UV A Sens in human erythroleukemic K562 cells. Here we have extended those studies by investigating the photopotency of UV A Sens in four haematological cell lines, namely, K562, T-cell leukaemic CEM-CCRF, P-glycoprotein overexpressing R100, and transformed B-lymphoblastoid cell lines (LCL) cells. In addition, we investigated the effects of suberoylanilide hydroxamic acid in combination with UV A Sens. Using γH2AX as the endpoint, our findings indicate that UV A Sens-induced phototoxicity in all four of the haematological cell lines. The addition of suberoylanilide hydroxamic acid augmented the photopotency of UV A Sens highlighting the potential clinical applicability of combination therapies.

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Histone Deacetylase Inhibitor Sodium Butyrate Enhances the Cell Killing Effect of Psoralen plus UVA by Attenuating Nucleotide Excision Repair

Cited by 27 publications

References 49 publications

The Inhibitor of Histone Deacetylases Sodium Butyrate Enhances the Cytotoxicity of Mitomycin C

The Inhibitor of Histone Deacetylases Sodium Butyrate Enhances the Cytotoxicity of Mitomycin C

Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C

Combination Phototherapy with a Histone Deacetylase Inhibitor and a Potent DNA-Binding Bibenzimidazole: Effects in Haematological Cell Lines

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