DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yongseok Choi | - |
dc.contributor.author | Song Kyu Park | - |
dc.contributor.author | Hwan Mook Kim | - |
dc.contributor.author | Jong Soon Kang | - |
dc.contributor.author | Yeo Dae Yoon | - |
dc.contributor.author | S B Han | - |
dc.contributor.author | J W Han | - |
dc.contributor.author | J S Yang | - |
dc.contributor.author | G Han | - |
dc.date.accessioned | 2017-04-19T09:12:13Z | - |
dc.date.available | 2017-04-19T09:12:13Z | - |
dc.date.issued | 2008 | - |
dc.identifier.issn | I000-0028 | - |
dc.identifier.uri | 10.3858/emm.2008.40.5.574 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/8707 | - |
dc.description.abstract | In light of the anti-inflammatory properties of histone deacetylase (HDAC) inhibitors, such as suberoylanilide hydroxamic acid (SAHA) and trichostatin A (TSA), we examined a new HDAC inhibitor KBH-A42 for its anti-inflammatory activities. KBH-A42 showed noteworthy anti-inflammatory properties in vitro via suppression of the production of TNF-α, a proinflammatory cytokine, and nitric oxide (NO), a proinflammatory effector molecule, in LPS-stimulated RAW264.7 cells and peritoneal macrophages. It also inhibited TNF-α production in vivo as demonstrated in a LPS-induced mouse endotoxemia model. The levels of TNF-α, IL-1β, IL-6 and iNOS mRNAs determined by RT-PCR propose that the inhibition of these pro-inflammatory mediators by KBH-A42 resulted from inhibiting expression of these genes. However, the EMSA study to see the effect of KBH-A42 on the binding of NF-κB, a transcription factor, to a specific DNA sequence showed that the binding of NF-κB to DNA was not changed regardless of increasing the concentration of KBH-A42 in the presence and absence of LPS stimulation. Interestingly, DNA binding of another transcription factor AP-1 dose-dependently increased by KBH-A42. KBH-A42 differentially regulated the phosphorylation of MAP kinases. While the phosphprylation of ERK1/2 and SAPK/JNK was not affected by KBH-A42, the phosphorylation of p38 decreased by KBH-A42. These results showed that KBH-A42 inhibits production of proinflammatory cytokines in macrophages by decreasing their mRNA levels, and p38 kinase is involved in the KBH-A42-mediated inhibition.n light of the anti-inflammatory properties of histone deacetylase (HDAC) inhibitors, such as suberoylanilide hydroxamic acid (SAHA) and trichostatin A (TSA), we examined a new HDAC inhibitor KBH-A42 for its anti-inflammatory activities. KBH-A42 showed noteworthy anti-inflammatory properties in vitro via suppression of the production of TNF-α, a proinflammatory cytokine, and nitric oxide (NO), a proinflammatory effector molecule, in LPS-stimulated RAW264.7 cells and peritoneal macrophages. It also inhibited TNF-α production in vivo as demonstrated in a LPS-induced mouse endotoxemia model. The levels of TNF-α, IL-1β, IL-6 and iNOS mRNAs determined by RT-PCR propose that the inhibition of these pro-inflammatory mediators by KBH-A42 resulted from inhibiting expression of these genes. However, the EMSA study to see the effect of KBH-A42 on the binding of NF-κB, a transcription factor, to a specific DNA sequence showed that the binding of NF-κB to DNA was not changed regardless of increasing the concentration of KBH-A42 in the presence and absence of LPS stimulation. Interestingly, DNA binding of another transcription factor AP-1 dose-dependently increased by KBH-A42. KBH-A42 differentially regulated the phosphorylation of MAP kinases. While the phosphprylation of ERK1/2 and SAPK/JNK was not affected by KBH-A42, the phosphorylation of p38 decreased by KBH-A42. These results showed that KBH-A42 inhibits production of proinflammatory cytokines in macrophages by decreasing their mRNA levels, and p38 kinase is involved in the KBH-A42-mediated inhibition. | - |
dc.publisher | Springer-Nature Pub Group | - |
dc.title | Histone deacetylase inhibitor KBH-A42 inhibits cytokine production in RAW 264.7 macrophage cells and in vivo endotoxemia model | - |
dc.title.alternative | Histone deacetylase inhibitor KBH-A42 inhibits cytokine production in RAW 264.7 macrophage cells and in vivo endotoxemia model | - |
dc.type | Article | - |
dc.citation.title | Experimental and Molecular Medicine | - |
dc.citation.number | 5 | - |
dc.citation.endPage | 581 | - |
dc.citation.startPage | 574 | - |
dc.citation.volume | 40 | - |
dc.contributor.affiliatedAuthor | Song Kyu Park | - |
dc.contributor.affiliatedAuthor | Hwan Mook Kim | - |
dc.contributor.affiliatedAuthor | Jong Soon Kang | - |
dc.contributor.affiliatedAuthor | Yeo Dae Yoon | - |
dc.contributor.alternativeName | 최용석 | - |
dc.contributor.alternativeName | 박성규 | - |
dc.contributor.alternativeName | 김환묵 | - |
dc.contributor.alternativeName | 강종순 | - |
dc.contributor.alternativeName | 윤여대 | - |
dc.contributor.alternativeName | 한상배 | - |
dc.contributor.alternativeName | 한증환 | - |
dc.contributor.alternativeName | 양지선 | - |
dc.contributor.alternativeName | 한균희 | - |
dc.identifier.bibliographicCitation | Experimental and Molecular Medicine, vol. 40, no. 5, pp. 574-581 | - |
dc.identifier.doi | 10.3858/emm.2008.40.5.574 | - |
dc.subject.keyword | Anti-inflammatory agents | - |
dc.subject.keyword | Histone deacetylases | - |
dc.subject.keyword | NF-κ B | - |
dc.subject.keyword | Nitric oxide | - |
dc.subject.keyword | Transcription factor AP-1 | - |
dc.subject.keyword | Tumor necrosis factor-α | - |
dc.subject.keyword | Vorinostat | - |
dc.subject.local | Anti-inflammatory agents | - |
dc.subject.local | anti-inflammatory agent | - |
dc.subject.local | Histone deacetylase | - |
dc.subject.local | histone deacetylase (HDAC) | - |
dc.subject.local | Histone deacetylases | - |
dc.subject.local | histone deacetylase | - |
dc.subject.local | Nuclear factor-kappa B | - |
dc.subject.local | nuclear factor κB | - |
dc.subject.local | Nf-κb | - |
dc.subject.local | NF-kB | - |
dc.subject.local | nuclear factor kappa B | - |
dc.subject.local | NF-κB (nuclear factor kappa-B) | - |
dc.subject.local | NF-kappaB | - |
dc.subject.local | Nuclear factor-κb | - |
dc.subject.local | NF-κ B | - |
dc.subject.local | NF-κB | - |
dc.subject.local | NF-kappa B | - |
dc.subject.local | Nuclear factor κB (NF-κB) | - |
dc.subject.local | Nuclear factor κB | - |
dc.subject.local | NFκB | - |
dc.subject.local | Nf-κB | - |
dc.subject.local | Nuclear factor-κB | - |
dc.subject.local | nuclear factorκB | - |
dc.subject.local | Nuclear factor (NF)-κB | - |
dc.subject.local | Nuclear factor kappa B | - |
dc.subject.local | nuclear factor-κB | - |
dc.subject.local | NF-ΚB | - |
dc.subject.local | Nuclear factor-kappa B (NF-κB) | - |
dc.subject.local | Nuclear factor-kappaB | - |
dc.subject.local | nuclear factor-kappaB | - |
dc.subject.local | nuclear factor-kappaB (NF-κB) | - |
dc.subject.local | NFkappaB | - |
dc.subject.local | Nuclear factor kappaB | - |
dc.subject.local | NO | - |
dc.subject.local | nitric oxide | - |
dc.subject.local | nitric oxide (NO) | - |
dc.subject.local | Nitric oxide | - |
dc.subject.local | NO (Nitric oxide) | - |
dc.subject.local | nitric oxide. | - |
dc.subject.local | Nitric oxid | - |
dc.subject.local | Nitric oxide (NO) | - |
dc.subject.local | Transcription factor AP-1 | - |
dc.subject.local | Tumor necrosis fa tor-α | - |
dc.subject.local | TNFα | - |
dc.subject.local | Tumor necrosis factor (TNF)-α | - |
dc.subject.local | Tnf-α | - |
dc.subject.local | TNF-a | - |
dc.subject.local | TNF-alpha | - |
dc.subject.local | Tumor necrosis factor-α | - |
dc.subject.local | tumor necrosis factor-alpha | - |
dc.subject.local | TNFa | - |
dc.subject.local | Tumor necrosis factor alpha | - |
dc.subject.local | Tumor necrosis factor-alpha | - |
dc.subject.local | TNF-α | - |
dc.subject.local | tumor necrosis factor-α | - |
dc.subject.local | Vorinostat | - |
dc.description.journalClass | Y | - |
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