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- 저자 : Yonghui Yang (검색결과 5 건)
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Epigenetic silencing of UBXN8 contributes to leukemogenesis in t(8;21) acute myeloid leukemia
Yang Erna,Guan Wei,Gong Desheng,Li Jieying,Han Caixia,Zhang Juan,Wang Hong,Kang Synat,Gao Xuefeng,Li Yonghui,Yu Li 생화학분자생물학회 2021 Experimental and molecular medicine Vol.53 No.-
The formation of the RUNX1-RUNX1T1 fusion protein, resulting from the t(8;21) translocation, is considered to be one of the initiating events of t(8;21) acute myeloid leukemia (AML). However, the mechanisms of the oncogenic mechanism of RUNX1- RUNX1T1 remain unclear. In this study, we found that RUNX1-RUNX1T1 triggers the heterochromatic silencing of UBXN8 by recognizing the RUNX1-binding sites and recruiting chromatin-remodeling enzymes to the UBXN8 promoter region. Decitabine, a specific inhibitor of DNA methylation, upregulated the expression of UBXN8 in RUNX1-RUNX1T1+ AML cell lines. Overexpression of UBXN8 inhibited the proliferation and colony-forming ability of and promoted cell cycle arrest in t(8;21) AML cell lines. Enhancing UBXN8 levels can significantly inhibit tumor proliferation and promote the differentiation of RUNX1-RUNX1T1+ cells in vivo. In conclusion, our results indicated that epigenetic silencing of UBXN8 via methylation of its promoter region mediated by the RUNX1- RUNX1T1 fusion protein contributes to the leukemogenesis of t(8;21) AML and that UBXN8 targeting may be a potential therapeutic strategy for t(8;21) AML. The formation of the RUNX1-RUNX1T1 fusion protein, resulting from the t(8;21) translocation, is considered to be one of the initiating events of t(8;21) acute myeloid leukemia (AML). However, the mechanisms of the oncogenic mechanism of RUNX1-RUNX1T1 remain unclear. In this study, we found that RUNX1-RUNX1T1 triggers the heterochromatic silencing of UBXN8 by recognizing the RUNX1-binding sites and recruiting chromatin-remodeling enzymes to the UBXN8 promoter region. Decitabine, a specific inhibitor of DNA methylation, upregulated the expression of UBXN8 in RUNX1-RUNX1T1 + AML cell lines. Overexpression of UBXN8 inhibited the proliferation and colony-forming ability of and promoted cell cycle arrest in t(8;21) AML cell lines. Enhancing UBXN8 levels can significantly inhibit tumor proliferation and promote the differentiation of RUNX1-RUNX1T1 + cells in vivo. In conclusion, our results indicated that epigenetic silencing of UBXN8 via methylation of its promoter region mediated by the RUNX1-RUNX1T1 fusion protein contributes to the leukemogenesis of t(8;21) AML and that UBXN8 targeting may be a potential therapeutic strategy for t(8;21) AML.
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Upregulation of Fas in epithelial ovarian cancer reverses the development of resistance to Cisplatin
( Fan Yang ),( Wang Long ),( Han Xuechuan ),( Liu Xueqin ),( Ma Hongyun ),( Ding Yonghui ) 생화학분자생물학회(구 한국생화학분자생물학회) 2015 BMB Reports Vol.48 No.1
This study was to investigate the role of Fas in the developmentof Cisplatin-resistant ovarian cancer. On the cellularlevel, Fas expression was significantly reduced in Cisplatinresistant A2780 (A2780/CP) cells compared with A2780 cells. Fas silence with siRNA would promote tumor cell linesproliferation, facilitate tumor cell cycle transition of G1/S,prevent cell apoptosis, and promote cell migration. Expressionof drug resistance gene was negatively correlated to Fas. Innude mice metastasis model of human ovarian carcinoma bysubcutaneous transplantation, after Ad-Fas injected intratumorly,we found that upregulation of Fas could inhibit transplantationtumor tissue growth and reduce the expression of drugresistance gene. Our results indicated that upregulation of Fasin epithelial ovarian cancer reversed the development ofresistance to Cisplatin. In conclusion, our findings suggestedthat Fas might act as a promising therapeutic target for improvementof the sensibility to Cisplatin in ovarian cancer.
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Xin Liu,Chuang Gao,Huanqing Wang,Libing Wu,Yonghui Yang 제어·로봇·시스템학회 2020 International Journal of Control, Automation, and Vol.18 No.8
In this study, an adaptive neural backstepping control scheme is proposed for a class of nonstrict-feedback time-delay systems with input saturation, full-state constraints and unknown disturbances. A structural property of radial basis function neural network is presented to deal with the design from the nonstrict-feedback formation. This method does not require the parameter separation technique and its assumption. With the help of the Lyapunov-Krasovskii functionals and Young’s inequalities, the effects of time delays are compensated, and the unknown disturbances are eliminated in the design process. The barrier Lyapunov function (BLF) is applied to arrest the violation of the full-state constraints. To overcome the problem of input saturation nonlinearity, the smooth nonaffine function of the control input signal is adopted to approach the input saturation function. Moreover, an adaptive backstepping neural control strategy is proposed. The proposed adaptive neural controller ensures that all the closed-loop signals are semi-globally uniformly ultimately bounded (SGUUB). Furthermore, the tracking error can converge to a small neighborhood of the origin. The simulation result shows the effectiveness of this method.
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Yin Qin,Batbatan Christopher G.,Li Yongxing,Zhang Yonghui,Yang Qiuming,Xiao Anfeng 한국미생물·생명공학회 2024 Journal of microbiology and biotechnology Vol.34 No.1
In this study, carrageenase immobilization was evaluated with a concise and efficient strategy. Pomelo peel cellulose (PPC) modified by polyethyleneimine (PEI) using the physical absorption method was used as a carrier to immobilize carrageenase and achieved repeated batch catalysis. In addition, various immobilization and reaction parameters were scrutinized to enhance the immobilization efficiency. Under the optimized conditions, the enzyme activity recovery rate was more than 50% and 4.1 times higher than immobilization with non-modified pomelo peels. The optimum temperature and pH of carrageenase after immobilization by PEI-modified pomelo peel, at 60°C and 7.5 respectively, were in line with the free enzyme. The temperature resistance was reduced, inconsistent with free enzyme, and pH resistance was increased. A significant loss of activity (46.8%) was observed after reusing it thrice under optimal reaction conditions. In terms of stability, the immobilized enzyme conserved 76.0% of the initial enzyme activity after 98 days of storage. Furthermore, a modest decrease in the kinetic constant (Km) value was observed, indicating the improved substrate affinity of the immobilized enzyme. Therefore, modified pomelo peel is a verified and promising enzyme immobilization system for the synthesis of inorganic solvents.
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