Epigenetic regulation of extracellular-superoxide dismutase in human monocytes

Kamiya, Tetsuro; Machiura, Masatomo; Makino, Junya; Hara, Hirokazu; Hozumi, Isao; Adachi, Tetsuo

doi:10.1016/j.freeradbiomed.2013.04.013

Cited by 38 publications

(41 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We previously reported that the expression of EC-SOD in basal human monocytic THP-1 cells was silenced, and attributed this to CpG hypermethylation within its promoter region. 20) As noted above, DNA methylation processes may be associated with CoCl 2 -elicited decreases in EC-SOD in COS7 cells; however, a treatment with 5-azacytidine, an inhibitor of DNMT, did not suppress these decreases (data not shown). These results indicate that CoCl 2 -elicited decreases in EC-SOD are regulated in a DNA methylation-independent manner.…”

Section: Discussionmentioning

confidence: 76%

“…After this treatment, histone proteins were collected and purified by the method described in our previous study. 20) In order to assess phospho-or total p38-MAPK levels, COS7 cells (seeded at 3.6×10…”

Section: Methodsmentioning

confidence: 99%

“…20) The abundance of EC-SOD promoter regions in ChIP precipitates was quantified using a PCR analysis. The primer sequences for EC-SOD were sense 5′-GTG GAG GCG AAG CAA TTC TA-3′; antisense 5′-CTG TTA GCG CGA GTG CAG GA-3′.…”

Section: Methodsmentioning

confidence: 99%

“…14) Moreover, EC-SOD expression is known to be regulated by epigenetics such as DNA methylation and histone modifications, particularly by histone deacetylation in human lung cancer, 28) human endothelial cells, 21) and monocytes/macrophages. 20) Accordingly, decreases in EC-SOD elicited by an exposure to CoCl 2 may be regulated by epigenetics. In order to elucidate the involvement of epigenetics in CoCl 2 -elicited decreases in EC-SOD, histone acetylation levels were measured after the exposure to CoCl 2 .…”

Section: Involvement Of Histone Deacetylation In Cocl 2 -Elicitedmentioning

confidence: 99%

“…14) Recent studies reported that epigenetics, such as DNA methylation and histone modifications, play pivotal roles in the progression of CKD, and some inhibitors of histone deacetylase (HDAC) exert beneficial effects against CKD. [15][16][17] Moreover, the expression of EC-SOD is known to be regulated by epigenetics in human lung cancer cells, 18,19) monocytes/macrophages, 20) and retina endothelial cells 21) ; however, limited information is currently available on EC-SOD regulation mechanisms in CKD models and the involvement of epigenetics.…”

mentioning

confidence: 99%

See 4 more Smart Citations

CoCl<sub>2</sub> Decreases EC-SOD Expression through Histone Deacetylation in COS7 Cells

Hattori

Kamiya

Hara

et al. 2016

Biological & Pharmaceutical Bulletin

Self Cite

View full text Add to dashboard Cite

Extracellular-superoxide dismutase (EC-SOD), one of the SOD isozymes, is negatively regulated under hypoxic conditions, and decreases in its expression may exacerbate vascular diseases. Moreover, epigenetics, such as DNA methylation and histone modifications, are known to play a critical role in the progression of cancer, type 2 diabetes, and atherosclerosis. We previously investigated the involvement of reactive oxygen species (ROS) and p38 mitogen-activated protein kinase (MAPK) in decreases in EC-SOD expression in hypoxic COS7 cells; however, the role of epigenetics in this process currently remains unknown. In the present study, we demonstrated that the hypoxia mimetic cobalt chloride (CoCl 2 ) decreased histone acetylation levels, and a pretreatment with 4-phenyl butyric acid (PBA), an inhibitor of histone deacetylase, significantly suppressed CoCl 2 -elicited histone deacetylation and decreases in EC-SOD. We found that CoCl 2 -elicited decreases in EC-SOD were accompanied by reductions in histone H3 acetylation levels within its promoter region. Furthermore, luteolin, a well-known flavonoid, significantly suppressed the CoCl 2 -elicited accumulation of ROS, p38-MAPK activation, and histone deacetylation. Collectively, the results of the present study showed for the first time that CoCl 2 decreases the expression of EC-SOD through its deacetylation and luteolin may be one of the seed compounds that maintain redox homeostasis, even under hypoxic conditions.

show abstract

Section: Discussionmentioning

confidence: 76%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Involvement Of Histone Deacetylation In Cocl 2 -Elicitedmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

CoCl<sub>2</sub> Decreases EC-SOD Expression through Histone Deacetylation in COS7 Cells

Hattori

Kamiya

Hara

et al. 2016

Biological & Pharmaceutical Bulletin

Self Cite

View full text Add to dashboard Cite

show abstract

Imperative connotation of SODs in cancer: Emerging targets and multifactorial role of action

Panda,

Tripathy,

Patra

et al. 2024

IUBMB Life

View full text Add to dashboard Cite

Superoxide dismutase (SOD) is a crucial enzyme responsible for the redox homeostasis inside the cell. As a part of the antioxidant defense system, it plays a pivotal role in the dismutation of the superoxide radicals () generated mainly by the oxidative phosphorylation, which would otherwise bring out the redox dysregulation, leading to higher reactive oxygen species (ROS) generation and, ultimately, cell transformation, and malignancy. Several studies have shown the involvement of ROS in a wide range of human cancers. As SOD is the key enzyme in regulating ROS, any change, such as a transcriptional change, epigenetic remodeling, functional alteration, and so forth, either activates the proto‐oncogenes or aberrant signaling cascades, which results in cancer. Interestingly, in some cases, SODs act as tumor promoters instead of suppressors. Furthermore, SODs have also been known to switch their role during tumor progression. In this review, we have tried to give a comprehensive account of SODs multifactorial role in various human cancers so that SODs‐based therapeutic strategies could be made to thwart cancers.

show abstract

Regulation of lysyl oxidase expression in THP‐1 cell‐derived M2‐like macrophages

Takemoto

Kamiya

Atobe

et al. 2021

J of Cellular Biochemistry

Self Cite

View full text Add to dashboard Cite

Lysyl oxidase (LOX) is a copper‐containing enzyme and its overexpression in tumor tissues promote tumor metastasis through the crosslinking of extracellular matrix. Our previous report demonstrated that LOX expression is significantly increased in human leukemic THP‐1 cell‐derived M2‐like macrophages, and histone modification plays a key role in its induction. However, the rigorous mechanism of LOX regulation remains unclear. In this study, we investigated the role of functional transcription factors, hypoxia‐inducible factor 1α (HIF1α), signal transducer and activator of transcription 3 (STAT3) and forkhead box O1 (FOXO1) in LOX regulation in M2‐like macrophages. HIF1α expression was significantly increased in M2‐like macrophages, and HIF1α inhibitor, TX402, suppressed LOX induction. The significant STAT3 activation was also observed in M2‐like macrophages. Additionally, LOX induction was canceled in the presence of STAT3 inhibitor, S3I‐201, suggesting that HIF1α and STAT3 pathways play a critical role in LOX induction. On the other hand, our ChIP results clearly indicated that the enrichment of FOXO1 within the lox promoter region was dramatically decreased in M2‐like macrophages. In this context, knockdown of FOXO1 further enhanced LOX induction. LOX induction and HIF1α binding to the lox promoter region were suppressed in FOXO1‐overexpressed cells, suggesting that the FOXO1 binding to the lox promoter region counteracted HIF1α binding to that region. Overall, the present data suggested that both of HIF1α and STAT3 were required for LOX induction in M2‐like macrophages, and loss of FOXO1 within the lox promoter region facilitated HIF1α binding to that region which promoted LOX induction.

show abstract

Epigenetic regulation of extracellular-superoxide dismutase in human monocytes

Cited by 38 publications

References 46 publications

CoCl<sub>2</sub> Decreases EC-SOD Expression through Histone Deacetylation in COS7 Cells

CoCl<sub>2</sub> Decreases EC-SOD Expression through Histone Deacetylation in COS7 Cells

Imperative connotation of SODs in cancer: Emerging targets and multifactorial role of action

Regulation of lysyl oxidase expression in THP‐1 cell‐derived M2‐like macrophages

Contact Info

Product

Resources

About