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

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 b...

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Autores principales: Li, Nan, Han, Zhenzhen, Li, Lin, Zhang, Bing, Liu, Zhidong, Li, Jiawei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5973426/
https://www.ncbi.nlm.nih.gov/pubmed/29872263
http://dx.doi.org/10.2147/DDDT.S160524
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author Li, Nan
Han, Zhenzhen
Li, Lin
Zhang, Bing
Liu, Zhidong
Li, Jiawei
author_facet Li, Nan
Han, Zhenzhen
Li, Lin
Zhang, Bing
Liu, Zhidong
Li, Jiawei
author_sort Li, Nan
collection PubMed
description 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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spelling pubmed-59734262018-06-05 The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles Li, Nan Han, Zhenzhen Li, Lin Zhang, Bing Liu, Zhidong Li, Jiawei Drug Des Devel Ther Original Research 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. Dove Medical Press 2018-05-23 /pmc/articles/PMC5973426/ /pubmed/29872263 http://dx.doi.org/10.2147/DDDT.S160524 Text en © 2018 Li et al. This work is published and licensed by Dove Medical Press Limited The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed.
spellingShingle Original Research
Li, Nan
Han, Zhenzhen
Li, Lin
Zhang, Bing
Liu, Zhidong
Li, Jiawei
The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title_full The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title_fullStr The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title_full_unstemmed The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title_short The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
title_sort anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5973426/
https://www.ncbi.nlm.nih.gov/pubmed/29872263
http://dx.doi.org/10.2147/DDDT.S160524
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