Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 채영규 | - |
dc.date.accessioned | 2018-03-13T10:04:29Z | - |
dc.date.available | 2018-03-13T10:04:29Z | - |
dc.date.issued | 2013-11 | - |
dc.identifier.citation | MOLECULAR IMMUNOLOGY, 권: 56, 호: 1-2, 페이지: 113-122 | en_US |
dc.identifier.issn | 0161-5890 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0161589013001648?via%3Dihub | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/46336 | - |
dc.description.abstract | JMJD3, a Jumonji C family histone demethylase, plays an important role in the regulation of inflammation induced by the transcription factor nuclear factor-kappa B (NF-kappa B) in response to various stimuli. JMJD3 is a histone-3 lysine-27 trimethylation (H3K27me3) demethylase, a histone mark associated with transcriptional repression and activation of a diverse set of genes. The present study assessed stable JMJD3 knockdown (KD)-dependent proteomic profiling in human leukemia monocyte (THP-1) cells to analyze the JMJD3-mediated differential changes of marker expression in inflammatory cells. To analyze the protein expression profile of tumor necrosis factor-alpha (TNF-alpha)-stimulated JMJD3-kd THP-1 cells, we employed matrix-assisted-laser-desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). Additionally, Ingenuity Pathways Analysis (IPA) was applied to establish the molecular networks. A comparative proteomic profile was determined in TNF-alpha-treated both of JMJD3-kd THP-1 cells and THP-1 scrambled (sc) cells. The expression of tripartite motif protein (TRIMS), glutathione peroxidase (GPx), glia maturation factor-gamma (GMFG), caspase recruitment domain family, member 14 (CARMA2), and dUTP pyrophosphatase were significantly down-regulated, whereas heat shock protein beta-1 (HspB1) and prohibition were significantly up-regulated in JMJD3-kd THP-1 cells. The molecular and signaling networks of the differentially expressed proteins in JMJD3-kd THP-1 cells were determined by IPA. The molecular network signatures and functional proteomics obtained in this study may facilitate the suppression of different key inflammatory regulators through JMJD3-attenuation, which would be crucial to evaluate potential therapeutic targets and to elucidate the molecular mechanism of JMJD3-kd dependent effects in THP-1 cells. (C) 2013 Elsevier Ltd. All rights reserved. | en_US |
dc.description.sponsorship | This work was supported by the National Research Foundation of Korea Grant funded by the Korean Government (No. 2012-0009212). | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier Science B.V., Amsterdam. | en_US |
dc.subject | Inflammation | en_US |
dc.subject | Ingenuity Pathway Analysis (IPA) | en_US |
dc.subject | JMJD3 | en_US |
dc.subject | MALDI-TOF MS | en_US |
dc.subject | NF-kappa B | en_US |
dc.subject | THP-1 cell | en_US |
dc.title | Proteomic changes induced by histone demethylase JMJD3 in TNF alpha-treated human monocytic (THP-1) cells | en_US |
dc.type | Article | en_US |
dc.relation.volume | 55 | - |
dc.identifier.doi | 10.1016/j.molimm.2013.04.013 | - |
dc.relation.page | 113-122 | - |
dc.relation.journal | MOLECULAR IMMUNOLOGY | - |
dc.contributor.googleauthor | Das, Amitabh | - |
dc.contributor.googleauthor | Das, Nando Dulal | - |
dc.contributor.googleauthor | Jung, Kyoung Hwa | - |
dc.contributor.googleauthor | Park, Ji Hyun | - |
dc.contributor.googleauthor | Lee, Hyung Tae | - |
dc.contributor.googleauthor | Han, DalMur | - |
dc.contributor.googleauthor | Choi, Mi Ran | - |
dc.contributor.googleauthor | Kang, Sung Chul | - |
dc.contributor.googleauthor | Chai, Young Gyu | - |
dc.relation.code | 2013011341 | - |
dc.sector.campus | S | - |
dc.sector.daehak | GRADUATE SCHOOL[S] | - |
dc.sector.department | DEPARTMENT OF BIONANOTECHNOLOGY | - |
dc.identifier.pid | ygchai | - |
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