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- 저자 : Liu Yafang (검색결과 2 건)
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Role of Estrogen Receptor-α in the Regulation of Claudin-6 Expression in Breast Cancer Cells
Liu Yafang,Wu Qiong,Ren Yue,Xu Xiaoming,Yu Lina,Zhang Mingzi,Zhang Ting,Li Yulin,Quan Chengshi 한국유방암학회 2011 Journal of breast cancer Vol.14 No.1
Purpose: In our previous studies we showed that upregulating claudin-6 (CLDN6) expression may contribute to preventing breast cancer, and that 17β-estradiol induces a concentration- and time-related effect on CLDN6 mRNA and protein expression in MCF-7 cells. However, the mechanisms of 17β-estradiol regulation of CLDN6 are still unclear. We determined the role of estrogen receptors in the regulation of CLDN6 expression in human breast cancer tissues and a cell line. Methods: CLDN6, estrogen receptor alpha (ERα) and estrogen receptor beta (ERβ) expression in breast cancer tissues were examined using immunohistochemistry. The human breast cancer cell line, MCF-7, which expresses ERα but not ERβ was used. CLDN6 and ERα expression were measured by reverse transcriptase-PCR, Western blotting and immunofluorescent staining. Treatments with propyl pyrazole triol (PPT) and ICI 182, 780 (ICI) were performed. Results: The results revealed that CLDN6 expression was related to ERα in breast cancer tissues (p=0.033). PPT, an ERα-selective ligand, upregulated CLDN6 expression at 10^(-5) mol/L after 24 hours. The effect of PPT on regulating CLDN6 expression in MCF-7 cells was blocked by ICI. Conclusion: These findings suggest that Erα reulates CLDN6 expression in breast cancer tissues and that 17β- estradiol induces CLDN6 expression through an ERα pathway in MCF-7 cells.
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Prediction of Cellulose Crystallinity in Liquid Phase Using CBM-GFP Probe
Xiaoyu Guo,Fan Yang,Huixue Liu,Yingmin Hou,Yafang Wang,Jie Sun,Xiaoyi Chen,Yanan Liu,Xianzhen Li 한국고분자학회 2019 Macromolecular Research Vol.27 No.4
Carbohydrate-binding modules (CBMs) have been developed to investigate the presence of crystalline and amorphous regions of cellulose. However, systematic and quantitative assessment of cellulose crystallinity using such non-hydrolytic fusion proteins in liquid phase has not been reported. In this work, cellulose directed CBM probes containing a green fluorescent protein (GFP) were constructed and named CG17, CG28, and CG2a. The probe binding condition was determined as incubating 30 μg/mL probes in 10 mM phosphate buffer at 30oC for 60 min. Under the optimized condition, the linear correlations between CBM probe binding capability and X-ray diffraction (XRD) crystallinity were well established. Using linear regression equations, the crystallinity of several cellulosic materials was well calculated. Amorphous component and cellulosic surface area probably had a less effect on binding capability of CG2a than that of CG17 and CG28. Therefore, crystalline-region specific probe CG2a should be an efficient tool for interpreting the crystallinity of cellulosic materials.
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