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소성준,Song Lee,Yeonmi Lee,Jongsuk Han,Soonsuk Kang,Jiwan Choi,Bitnara Kim,Deokhoon Kim,유현주,In-Kyong Shim,Ju-Yun Oh,Yu-Na Lee,Song Cheol Kim,Eunju Kang 생화학분자생물학회 2022 BMB Reports Vol.55 No.9
Diabetes mellitus (DM) is a serious disease in which blood sugarlevels rise abnormally because of failed insulin production ordecreased insulin sensitivity. Although many studies are beingconducted for the treatment or early diagnosis of DM, it is notfully understood how mitochondrial genome (mtDNA) abnormalitiesappear in patients with DM. Here, we induced iPSCs fromfibroblasts, PBMCs, or pancreatic cells of three patients with type2 DM (T2D) and three patients with non-diabetes counterpart. The mtDNA mutations were detected randomly without anytendency among tissues or patients. In T2D patients, 62% (21/34)of iPSC clones harbored multiple mtDNA mutations, of which37% were homoplasmy at the 100% mutation level comparedto only 8% in non-diabetes. We next selected iPSC clones thatwere a wild type or carried mutations and differentiated into pancreaticcells. Oxygen consumption rates were significantly lowerin cells carrying mutant mtDNA. Additionally, the mutant cellsexhibited decreased production of insulin and reduced secretionof insulin in response to glucose. Overall, the results suggest thatscreening mtDNA mutations in iPSCs from patients with T2Dis an essential step before pancreatic cell differentiation for diseasemodeling or autologous cell therapy.
Soluble Expression and Purification of Bioactive Interleukin 33 in E. coli
Bich Hang Do,박상수,Grace G. Kwon,NGUYEN MINH TAN,강효정,송정아,유지원,Anh Ngoc Nguyen,장재평,장미희,이선주,소성준,심성락,진종화,이경진,Mark J Osborn,최한 한국생물공학회 2017 Biotechnology and Bioprocess Engineering Vol.22 No.3
Interleukin-33 (IL-33) is one of the important alarmins of the immune system and possesses dual functions as an anti- or pro-inflammatory molecule. The production of this cytokine in E. coli is hampered by the insoluble expression in the cytoplasm, resulting in inclusion body formation. In this study, the expression of IL-33 was optimized by fusing the N-terminus of IL-33 with several solubilizing tags that act as chaperones for proper protein folding: maltose binding protein (MBP), b´a´ domain of protein disulfide isomerase (PDIb´a´) and glutathione Stransferase (GST). The expression of the fusion proteins was stimulated by 0.5 mM IPTG at different temperatures, 37, 30, 25, and 18oC. As a result, IL-33 was expressed highly and in soluble form in the cytoplasm of E. coli when fused with MBP or PDIb´a´ tags in the presence of 0.5 mM IPTG at 25 or 30oC. We describe a simple purification procedure of IL-33 from the PDIb´a´-IL-33 construct using immobilized metal affinity chromatography (IMACs) with supplementary of tobacco etch virus (TEV) protease for tag removal. The high bioactivity of purified IL-33 on the proliferation and activation of macrophages was confirmed by MTT and nitrite releasing assays using RAW 264.7 These data show an improved method for producing high grade and yield IL-33.