The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
Authors Li N, Han Z, Li L, Zhang B, Liu Z, Li J
Received 21 December 2017
Accepted for publication 9 February 2018
Published 23 May 2018 Volume 2018:12 Pages 1399—1411
Checked for plagiarism Yes
Review by Single-blind
Peer reviewer comments 2
Editor who approved publication: Dr Anastasios Lymperopoulos
Nan Li,1–3,* Zhenzhen Han,1,2,4,* Lin Li,1,2 Bing Zhang,1–3 Zhidong Liu,1–3 Jiawei Li1,2
1Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin, People’s Republic of China; 2Institute of Traditional Chinese Medicine,Tianjin University of Traditional Chinese Medicine, Tianjin, People’s Republic of China; 3Engineering Research Center of Modern Chinese Medicine Discovery and Preparation Technique, Ministry of Education, Tianjin University of Traditional Chinese Medicine, Tianjin, People’s Republic of China; 4Baokang Hospital, Tianjin University of Traditional Chinese Medicine, Tianjin, People’s Republic of China
*These authors contributed equally to this work
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.
Keywords: BA-SLNs, 2-DE patterns, nano-LC–MS/MS, IPA, SDS-PAGE
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