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RISS 인기검색어
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- 저자 : Haiwen Chen (검색결과 2 건)
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Chen Shoucheng,Huang Zhuwei,Visalakshan Rahul Madathiparambil,Liu Haiwen,Bachhuka Akash,Wu You,Dabare Panthihage Ruvini L.,Luo Pu,Liu Runheng,Gong Zhuohong,Xiao Yin,Vasilev Krasimir,Chen Zhuofan,Chen 한국생체재료학회 2023 생체재료학회지 Vol.27 No.00
Background: Transepithelial medical devices are increasing utilized in clinical practices. However, the damage of continuous natural epithelial barrier has become a major risk factor for the failure of epithelium-penetrating implants. How to increase the “epithelial barrier structures” (focal adhesions, hemidesmosomes, etc.) becomes one key research aim in overcoming this difficulty. Directly targeting the in situ “epithelial barrier structures” related proteins (such as fibronectin) absorption and functionalization can be a promising way to enhance interface-epithelial integration. Methods: Herein, we fabricated three plasma polymerized bio-interfaces possessing controllable surface chemistry. Their capacity to adsorb and functionalize fibronectin (FN) from serum protein was compared by Liquid Chromatography- Tandem Mass Spectrometry. The underlying mechanisms were revealed by molecular dynamics simulation. The response of gingival epithelial cells regarding the formation of epithelial barrier structures was tested. Results: Plasma polymerized surfaces successfully directed distinguished protein adsorption profiles from serum protein pool, in which plasma polymerized allylamine (ppAA) surface favored adsorbing adhesion related proteins and could promote FN absorption and functionalization via electrostatic interactions and hydrogen bonds, thus subsequently activating the ITG β1-FAK-mTOR signaling and promoting gingival epithelial cells adhesion. Conclusion: This study offers an effective perspective to overcome the current dilemma of the inferior interfaceepithelial integration by in situ protein absorption and functionalization, which may advance the development of functional transepithelial biointerfaces. Graphical Abstract: Tuning the surface chemistry by plasma polymerization can control the adsorption of fibronectin and functionalize it by exposing functional protein domains. The functionalized fibronectin can bind to human gingival epithelial cell membrane integrins to activate epithelial barrier structure related signaling pathway, which eventually enhances the formation of epithelial barrier structure.
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RBPJ contributes to acquired docetaxel resistance in prostate cancer cells
Li Xue,Zhenlong Wang,Hecheng Li,Zhaolun Li,Qi Chen,Peng Zhang,Haiwen Chen,Ziming Wang,Tie Chong,T. Chong 대한독성 유전단백체 학회 2017 Molecular & cellular toxicology Vol.13 No.3
Our previous work has shown that depletion of recombination signal-binding protein J (RBPJ) results in reduced cell growth in prostate cancer cells. In this study, we aimed to investigate the function of RBPJ in the chemoresistance of prostate cancer. The expression of RBPJ was quantified in docetaxel-resistant and parental prostate cancer cells. Loss- and gainof- function experiments were conducted to explore the regulatory role of RBPJ in prostate cancer sensitivity to docetaxel. The pro-apoptotic effect of RBPJ silencing was checked in docetaxel-resistant prostate cancer cells. We found that docetaxel-resistant PC3-DR and DU145- DR cells expressed 3-5-fold high levels of RBPJ than parental PC3 and DU145 cells. Short hairpin RNAmediated knockdown of RBPJ inhibited cell proliferation and colony formation and reversed docetaxel resistance in docetaxel-resistant prostate cancer cells. In contrast, overexpression of RBPJ promoted cell growth, colony formation, and docetaxel resistance in parental prostate cancer cells. Downregulation of RBPJ induced apoptosis in docetaxel-resistant cells, which was accompanied by enhanced cleavage of caspase-3. In addition, RBPJ silencing or overexpression markedly modulated the expression of the Bcl-2 family members including Bcl-2, Bcl-xL, Mcl-1, Bax, and Bak. Altogether, RBPJ contributes to acquisition of docetaxel resistance in prostate cancer cells and may thus represent a potential target for overcoming chemotherapeutic resistance in this malignancy.
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