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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.
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页码:1399 / 1411
页数:13
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