Chronic exposure to arsenite induces S100A8 and S100A9 expression in rat RBL-2H3 mast cells

Shimizu, Yuri; Fujishiro, Hitomi; Matsumoto, Kazuya; Sumi, Daigo; Satoh, Masahiko; Himeno, Seiichiro

doi:10.2131/jts.36.135

Cited by 3 publications

(4 citation statements)

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“…We previously showed that expression of S100A8 and S100A9 is upregulated by chronic exposure to As(III) in rat RBL-2H3 cells (6). In the present study, we first examined whether As(III) also induces S100A8 and S100A9 expression in other human-derived cell lines, including lung epithelial A549 cells, kidney carcinoma Caki-2 cells, immortalized skin keratinocytic HaCaT cells, embryonic kidney HEK293 cells, liver carcinoma HepG2 cells, immortalized T lymphocyte Jurkat cells, normal human epidermal keratinocytes (NHEK), leukemic monocyte lymphoma U937 cells, and immortalized bladder urothelial UROtsa cells.…”

Section: Resultsmentioning

confidence: 98%

“…We previously showed that S100A8 and S100A9 are upregulated in rat RBL-2H3 mast cells after chronic exposure to As(III) (6). To test whether this induction is restricted to RBL-2H3 cells, nine human-derived cell lines were exposed to As(III).…”

Section: Discussionmentioning

confidence: 99%

“…It was found that some S100 proteins, including S100A9, S100A10, S100A6 and S100A13, were upregulated in RBL-2H3 cells after chronic exposure to As(III). Among S100 proteins, the mRNA levels of S100A8 and S100A9 determined by real-time RT-PCR were highly upregulated following a 1-and 2-week exposure to As(III) (6). S100A8 and S100A9, which comprise a complex called calprotectin, are highly expressed in neutrophils, monocytes and activated macrophages.…”

Section: Introductionmentioning

confidence: 99%

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Involvement of Nrf2 activation in the upregulation of S100A9 by exposure to inorganic arsenite

Sumi

Shimizu

Himeno

2012

International Journal of Molecular Medicine

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Abstract. This study examined whether S100A8 and S100A9, which comprise a complex called calprotectin, are upregulated by exposure to sodium arsenite [As(III)] in nine lines of human-derived cells. HaCaT skin keratinocyte cells, U937 leukemic monocyte cells, and UROtsa urothelial cells showed increased mRNA levels of S100A8 and S100A9 after a 2-week exposure to As(III). To understand the mechanisms regulating S100A9 upregulation in response to As(III), we tested S100A9 promoter-dependent luciferase activity in HaCaT cells transfected with S100A9 promoter (-1000/+429)-fused luciferase cDNA. The results indicated that exposure to As(III) stimulated S100A9 promoter-dependent luciferase activity. In addition, the transcription NF-E2-related factor 2 (Nrf2) was strongly activated in HaCaT cells exposed to As(III). Since two putative antioxidant response elements were found in the S100A9 promoter (ARE1, 5'-ACAGGCAGGG-3' from -897 to -887; ARE2, 5'-ATCTTCCGGAG-3' from -78 to -67), we constructed deletion mutants of each ARE on S100A9 promoter-fused luciferase cDNA. The results indicated that ARE2 is the responsible element for the activation of S100A9 transcription in response to As(III). This report is the first to demonstrate that As(III) enhanced S100A8 and S100A9 expression in human-derived cells and As(III)-induced S100A9 expression is dependent on Nrf2 activation.

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Section: Resultsmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Involvement of Nrf2 activation in the upregulation of S100A9 by exposure to inorganic arsenite

Sumi

Shimizu

Himeno

2012

International Journal of Molecular Medicine

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“…S100a9, which encodes the S100A9 protein, was also ranked as having the third-lowest expression in both RBL-Mnr300 and RBL-Mnr1200 cells ( Supplementary Table 2). S100 family proteins commonly contain EF-hands for calcium-binding in their protein structure, and are involved in a variety of immunological responses (Shimizu et al, 2011;Foell et al, 2007;Marenholz et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

Down-regulation of S100A9 and S100A10 in manganese-resistant RBL-2H3 cells

et al. 2013

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Exposure to excess amounts of manganese causes toxic effects, including neurological symptoms such as Parkinsonism. However, endogenous factors involved in the protection against manganese toxicity remain unclear. Previously, we showed that rat basophilic leukemia RBL-2H3 cells are highly sensitive to MnCl₂ compared with other rat cell lines. To identify the genes involved in resistance to manganese toxicity, two lines of Mn-resistant cells showing resistance to 300 µM MnCl₂ (RBL-Mnr300) and 1200 µM MnCl₂ (RBL-Mnr1200) were developed from RBL-2H3 cells by a stepwise increase in MnCl₂ concentration in the medium. Microarray analyses were carried out to compare gene expression between parental RBL-2H3 cells and RBL-Mnr300 or RBL-Mnr1200 cells. Five genes exhibited more than 10-fold up-regulation in both RBL-Mnr300 and RBL-Mnr1200 cells, and 24 genes exhibited less than 0.1-fold down-regulation in both Mn-resistant cell lines. The S100a9 and S100a10 genes, encoding the calcium-binding S100A9 and S100A10 proteins, respectively, were found among the three most down-regulated genes in both Mn-resistant cell lines. The marked decreases in mRNA levels of S100a9 and S100a10 were confirmed by real-time RT-PCR analyses. Further characterization and comparison of these Mn-resistant cells may enable the identification of novel genes that play important roles in the modification of manganese toxicity.

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Molecular characterization of the porcine S100A6 gene and analysis of its expression in pigs infected with highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV)

et al. 2014

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Our previous microarray study revealed that S100A6 was significantly upregulated in porcine alveolar macrophages (PAMs) infected with highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV). In the present study, we cloned both cDNA and genomic DNA sequences of the gene. Transient transfection indicated that the porcine S100A6 protein was located in the nucleus and cytoplasm. Reverse transcription polymerase chain reaction (RT-PCR) revealed that the porcine S100A6 gene was highly expressed in the kidney and subcutaneous fat. Polyinosinic-polycytidylic acid [poly (I:C)] induced porcine S100A6 gene expression in PK-15 cells. Quantitative real-time PCR (Q-PCR) analysis further showed that the porcine S100A6 gene was upregulated in different cells and tissues of Tongcheng pigs infected with HP-PRRSV. Chromosome walking obtained the porcine S100A6 promoter region and then luciferase reporter assays confirmed its regulatory activities. We observed a putative NF-κB binding site in the core promoter region, which may explain the upregulation of porcine S100A6 in response to PRRSV. Transfection of NF-κB (p65 subunit) intensely induced the promoter activity of the porcine S100A6 gene, while an NF-κB inhibitor, pyrrolidine dithiocarbamate (PDTC), inhibited this activity. Furthermore, compared to its wild type, the promoter activity was significantly reduced when it contained a mutant NF-κB binding site. All these results provide a solid foundation to further investigate how S100A6 is involved in PRRSV infection.

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Chronic exposure to arsenite induces S100A8 and S100A9 expression in rat RBL-2H3 mast cells

Cited by 3 publications

References 31 publications

Involvement of Nrf2 activation in the upregulation of S100A9 by exposure to inorganic arsenite

Involvement of Nrf2 activation in the upregulation of S100A9 by exposure to inorganic arsenite

Down-regulation of S100A9 and S100A10 in manganese-resistant RBL-2H3 cells

Molecular characterization of the porcine S100A6 gene and analysis of its expression in pigs infected with highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV)

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