The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles

被引:10
|
作者
Li, Nan [1 ,2 ,3 ]
Han, Zhenzhen [1 ,2 ,4 ]
Li, Lin [1 ,2 ]
Zhang, Bing [1 ,2 ,3 ]
Liu, Zhidong [1 ,2 ,3 ]
Li, Jiawei [1 ,2 ]
机构
[1] Tianjin Univ Tradit Chinese Med, Tianjin State Key Lab Modern Chinese Med, Tianjin, Peoples R China
[2] Tianjin Univ Tradit Chinese Med, Inst Tradit Chinese Med, Tianjin, Peoples R China
[3] Tianjin Univ Tradit Chinese Med, Engn Res Ctr Modern Chinese Med Discovery & Prepa, Minist Educ, 88 Yuquan Rd, Tianjin 300193, Peoples R China
[4] Tianjin Univ Tradit Chinese Med, Baokang Hosp, Tianjin, Peoples R China
来源
关键词
BA-SLNs; 2-DE patterns; nano-LC-MS/MS; IPA; SDS-PAGE; HEAT-SHOCK PROTEINS; ALPHA-CRYSTALLIN; PROTEOMIC ANALYSIS; OXIDATIVE STRESS; NUCLEAR CATARACT; HSPB1; EYE; NETWORK; GAMMA; STATE;
D O I
10.2147/DDDT.S160524
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Purpose: The objective of this study was to investigate the effects of the solid lipid nanoparticles of baicalin (BA-SLNs) on an experimental cataract model and explore the molecular mechanism combined with bioinformatics analysis. Materials and methods: The transparency of lens was observed daily by slit-lamp and photography. Lenticular opacity was graded. Two-dimensional gel electrophoresis (2-DE) was employed to analyze the differential protein expression modes in each group. Proteins of interest were subjected to protein identification by nano-liquid chromatography tandem mass spectrometry (LC-MS/MS). Bioinformatics analysis was performed using the Ingenuity Pathway Analysis (IPA) online software to comprehend the biological implications of the proteins identified by proteomics. Results: At the end of the sodium selenite-induced cataract progression, almost all lenses from the model group developed partial nuclear opacity; however, all lenses were clear and normal in the blank group. There was no significant difference between the BA-SLNs group and the blank group. Many protein spots were differently expressed in 2-DE patterns of total proteins of lenses from each group, and 65 highly different protein spots were selected to be identified between the BA-SLNs group and the model group. A total of 23 proteins were identified, and 12 of which were crystalline proteins. Conclusion: We considered crystalline proteins to play important roles in preserving the normal expression levels of proteins and the transparency of lenses. The general trend in the BA-SLN-treated lenses' data showed that BA-SLNs regulated the protein expression mode of cataract lenses to normal lenses. Our findings suggest that BA-SLNs may be a potential therapeutic agent in treating cataract by regulating protein expression and may also be a strong candidate for future clinical research.
引用
收藏
页码:1399 / 1411
页数:13
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