Search

Your search keyword '"Xiao, Yechen"' showing total 37 results
Start Over Author "Xiao, Yechen"
37 results on '"Xiao, Yechen"'

20. High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli

Author

Huang Yadong, Qin Yuxia, Wan Xiaoshan, Zhang Yaofang, Fu Lianjun, Zhao Hongxin, Xiao Yechen, Wang Huiyan, Gao Hongchang, and Li Xiaokun

Subjects
Biotechnology, TP248.13-248.65
Abstract

Abstract Background Fibroblast growth factor 21 (FGF21) is a promising drug candidate to combat metabolic diseases. However, high-level expression and purification of recombinant FGF21 (rFGF21) in Escherichia coli (E. coli) is difficult because rFGF21 forms inclusion bodies in the bacteria making it difficult to purify and obtain high concentrations of bioactive rFGF21. To overcome this problem, we fused the FGF21 with SUMO (Small ubiquitin-related modifier) by polymerase chain reaction (PCR), and expressed the fused gene in E. coli BL21(DE3). Results By inducing with IPTG, SUMO-FGF21 was expressed at a high level. Its concentration reached 30% of total protein, and exceeded 95% of all soluble proteins. The fused protein was purified by DEAE sepharose FF and Ni-NTA affinity chromatography. Once cleaved by the SUMO protease, the purity of rFGF21 by high performance liquid chromatography (HPLC) was shown to be higher than 96% with low endotoxin level (in vivo animal experiments showed that rFGF21 produced by using this method, could decrease the concentration of plasma glucose in diabetic rats by streptozotocin (STZ) injection. Conclusions This study demonstrated that SUMO, when fused with FGF21, was able to promote its soluble expression of the latter in E. coli, making it more convenient to purify rFGF21 than previously. This may be a better method to produce rFGF21 for pharmaceutical research and development.

Published
2010
Full Text
View/download PDF

24. Loss of FGFR3 Accelerates Bone Marrow Suppression-Induced Hematopoietic Stem and Progenitor Cell Expansion by Activating FGFR1-ELK1-Cyclin D1 Signaling

Author

Ran, Qiuju, Guo, Chen, Sun, Chun, Liu, Qing, He, Haiting, Zhao, Wenjie, Zhang, Jizhou, and Xiao, Yechen

Abstract

•FGFR3 signaling is dispensable for steady-state hematopoiesis.•FGFR3 deficiency accelerates hematopoietic stem cell (HSC) recovery under bone marrow (BM) suppression.•FGFR3 inactivation accelerates HSC expansion via a cell-autonomous manner under BM suppression.•FGFR3 inactivation accelerates HSC expansion by activating FGFR1-ELK1-cyclin D1 signaling.•Loss of FGFR3 in hematopoietic cells inhibits in vivo leukemogenesis under BM suppression.

Published
2024
Full Text
View/download PDF

25. Transforming growth factor-beta-activated kinase 1 regulates natural killer cell-mediated cytotoxicity and cytokine production

Author

Rajasekaran, Kamalakannan, Chu, Haiyan, Kumar, Pawan, Xiao, Yechen, Tinguely, Mathew, Samarakoon, Asanga, Kim, Tae Whan, Li, Xiaoxia, Thakar, Monica S, Zhang, Jiwang, Malarkannan, Subramaniam, University of Zurich, and Malarkannan, Subramaniam

Subjects
1307 Cell Biology, 1303 Biochemistry, 10049 Institute of Pathology and Molecular Pathology, 1312 Molecular Biology, 610 Medicine & health
Published
2011

26. Expression and purification of soluble single-chain Fv against human fibroblast growth factor receptor 3 fused with Sumo tag in Escherichia coli

Author

Liu, Zixuan, primary, Zhang, Jizhou, additional, Fan, Hongqiong, additional, Yin, Ruofeng, additional, Zheng, Zhong, additional, Xu, Qian, additional, Liu, Qing, additional, He, Haiting, additional, Peng, Xiaofan, additional, Wang, XinXin, additional, Li, Xiaokun, additional, and Xiao, Yechen, additional

Published
2015
Full Text
View/download PDF

27. Sensitizing Acute Myeloid Leukemia Cells to Interferon-Induced Differentiation By Inhibiting RIP1/RIP3 Necroptotic Pathway

Author

Xin, Junping, primary, You, Dewen, additional, Volk, Andrew, additional, Zhang, Jun, additional, Li, Jing, additional, Schmidt, Rachel, additional, Ni, Allen, additional, Ng, Grace, additional, Wei, Wei, additional, Xia, Zhixin, additional, Xiao, Yechen, additional, Gutierrez, Rafael, additional, Pan, Jerry, additional, Breslin, Peter, additional, Chen, Haiyan, additional, Kuo, Paul C, additional, Nand, Sucha, additional, Zhang, Jianke, additional, Chen, Jianjun, additional, and Zhang, Jiwang, additional

Published
2014
Full Text
View/download PDF

28. Co-inhibition of NF-κB and JNK is synergistic in TNF-expressing human AML

Author

Volk, Andrew, primary, Li, Jing, additional, Xin, Junping, additional, You, Dewen, additional, Zhang, Jun, additional, Liu, Xinli, additional, Xiao, Yechen, additional, Breslin, Peter, additional, Li, Zejuan, additional, Wei, Wei, additional, Schmidt, Rachel, additional, Li, Xingyu, additional, Zhang, Zhou, additional, Kuo, Paul C., additional, Nand, Sucha, additional, Zhang, Jianke, additional, Chen, Jianjun, additional, and Zhang, Jiwang, additional

Published
2014
Full Text
View/download PDF

35. Cell-penetrating peptide TAT-mediated delivery of acidic FGF to retina and protection against ischemia–reperfusion injury in rats

Author

Wang, Yi, Lin, Haihuan, Lin, Shaoqiang, Qu, Jia, Xiao, Jian, Huang, Yadong, Xiao, Yechen, Fu, Xiaobing, Yang, Yongguang, and Li, Xiaokun

Subjects
cell-penetrating peptide, fibroblast growth factor, ischemia and reperfusion injury, retina, transactivator of transcription peptide
Abstract

The development of non-invasive ocular drug delivery systems is of practical importance in the treatment of retinal disease. In this study, we evaluated the efficacy of transactivator of transcription protein transduction domain (TAT-PTD, TAT49–57) as a vehicle to deliver acidic FGF (aFGF) to retina in rats. TAT-conjugated aFGF-His (TAT-aFGF-His) exhibited efficient penetration into the retina following topical administration to the ocular surface. Immunochemical staining with anti-His revealed that TAT-aFGF-His proteins were readily found in the retina (mainly in the ganglion cell layer) at 30 min. and remained detectable for at least 8 hrs after administration. In contrast, His+ proteins were undetectable in the retina after topical administration of aFGF-His, indicating that aFGF-His cannot penetrate the ocular barrier. Furthermore, TAT-aFGF-His, but not aFGF-His, mediated significant protection against retinal ischemia–reperfusion (IR) injury. After IR injury, retina from TAT-aFGF-His-treated rats showed better-maintained inner retinal layer structure, reduced apoptosis of retinal ganglion cells and improved retinal function compared to those treated with aFGF-His or PBS. These results indicate that conjugation of TAT to aFGF-His can markedly improve the ability of aFGF-His to penetrate the ocular barrier without impairing its biological function. Thus, TAT49–57 provides a potential vehicle for efficient drug delivery in the treatment of retinal disease.

Published
2009
Full Text
View/download PDF

37. Expression, Purification and Characterization of Recombinant Canine FGF21 in Escherichia coli.

Author

Zheng Z, Yang C, Yin R, Jiang J, He H, Wang X, Kan M, and Xiao Y

Subjects
Animals, Diabetes Mellitus, Experimental metabolism, Dog Diseases metabolism, Dogs, Escherichia coli drug effects, Fibroblast Growth Factors isolation & purification, Fibroblast Growth Factors metabolism, Isopropyl Thiogalactoside pharmacology, Metabolic Diseases veterinary, Mice, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Streptozocin, Blood Glucose analysis, Diabetes Mellitus, Experimental drug therapy, Escherichia coli genetics, Fibroblast Growth Factors administration & dosage, Fibroblast Growth Factors genetics
Abstract

The canine metabolic diseases, such as obesity and diabetes, have become a worldwide problem. Fibroblast growth factor 21 (FGF21) is a potent regulator which has many biological functions relative to metabolism regulation. It suggests that FGF21 plays important roles in regulating canine metabolic diseases. To acquire the recombinant canine FGF21 (rcFGF21) in Escherichia coli, the recombinant bacteria were induced by 0.5 mM IPTG for 16 hours at 16 °C, and the rcFGF21 protein was purified by Ni-NTA. 8 mg rcFGF21 was acquired from one liter bacteria. The rcFGF21 protein has specific immunoblot reactivity against anti-FGF21 and anti-His antibody. The in vivo experimental result showed that rcFGF21 can significantly reduce plasma glucose of STZ-induced diabetic mice.

Published
2016
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results