PMID- 23711388 OWN - NLM STAT- MEDLINE DCOM- 20130828 LR - 20211203 IS - 1872-9142 (Electronic) IS - 0161-5890 (Linking) VI - 56 IP - 1-2 DP - 2013 Nov TI - Proteomic changes induced by histone demethylase JMJD3 in TNF alpha-treated human monocytic (THP-1) cells. PG - 113-22 LID - S0161-5890(13)00164-8 [pii] LID - 10.1016/j.molimm.2013.04.013 [doi] AB - 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-kappaB) 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 (TRIM5), 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. CI - Copyright (c) 2013 Elsevier Ltd. All rights reserved. FAU - Das, Amitabh AU - Das A AD - Department of Molecular & Life Science, Hanyang University, Ansan, Republic of Korea. amitabhdas.kn@gmail.com FAU - Das, Nando Dulal AU - Das ND FAU - Jung, Kyoung Hwa AU - Jung KH FAU - Park, Ji Hyun AU - Park JH FAU - Lee, Hyung Tae AU - Lee HT FAU - Han, DalMuri AU - Han D FAU - Choi, Mi Ran AU - Choi MR FAU - Kang, Sung Chul AU - Kang SC FAU - Chai, Young Gyu AU - Chai YG LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20130525 PL - England TA - Mol Immunol JT - Molecular immunology JID - 7905289 RN - 0 (Antiviral Restriction Factors) RN - 0 (Carrier Proteins) RN - 0 (Cell Cycle Proteins) RN - 0 (NUDC protein, human) RN - 0 (Nuclear Proteins) RN - 0 (Proteome) RN - 0 (Tripartite Motif Proteins) RN - 0 (Tumor Necrosis Factor-alpha) RN - EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases) RN - EC 1.14.11.- (KDM6B protein, human) RN - EC 2.3.2.27 (TRIM5 protein, human) RN - EC 2.3.2.27 (Ubiquitin-Protein Ligases) SB - IM MH - Antiviral Restriction Factors MH - Blotting, Western MH - Carrier Proteins/genetics/metabolism MH - Cell Cycle Proteins/genetics/metabolism MH - Cell Line, Tumor MH - Electrophoresis, Gel, Two-Dimensional MH - Gene Expression Regulation, Neoplastic MH - Humans MH - Jumonji Domain-Containing Histone Demethylases/genetics/*metabolism MH - Monocytes/*drug effects/metabolism/pathology MH - Nuclear Proteins/genetics/metabolism MH - Proteome/genetics/metabolism MH - Proteomics/*methods MH - RNA Interference MH - Reverse Transcriptase Polymerase Chain Reaction MH - Signal Transduction/drug effects MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MH - Tripartite Motif Proteins MH - Tumor Necrosis Factor-alpha/*pharmacology MH - Ubiquitin-Protein Ligases EDAT- 2013/05/29 06:00 MHDA- 2013/08/29 06:00 CRDT- 2013/05/29 06:00 PHST- 2012/10/05 00:00 [received] PHST- 2013/03/16 00:00 [revised] PHST- 2013/04/23 00:00 [accepted] PHST- 2013/05/29 06:00 [entrez] PHST- 2013/05/29 06:00 [pubmed] PHST- 2013/08/29 06:00 [medline] AID - S0161-5890(13)00164-8 [pii] AID - 10.1016/j.molimm.2013.04.013 [doi] PST - ppublish SO - Mol Immunol. 2013 Nov;56(1-2):113-22. doi: 10.1016/j.molimm.2013.04.013. Epub 2013 May 25.