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      Quantitative Phosphoproteomic Comparison of Lens Proteins in Highly Myopic Cataract and Age-Related Cataract


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          To investigate and compare the lens phosphoproteomes in patients with highly myopic cataract (HMC) or age-related cataract (ARC).


          In this study, we undertook a comparative phosphoproteome analysis of the lenses from patients with HMC or ARC. Intact lenses from ARC and HMC patients were separated into the cortex and nucleus. After protein digestion, the phosphopeptides were quantitatively analyzed with TiO 2 enrichment and liquid chromatography-mass spectrometry. The potential functions of different phosphopeptides were assessed by Gene Ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analysis.


          In total, 522 phosphorylation sites in 164 phosphoproteins were identified. The number of phosphorylation sites was significantly higher in the cortex than in the nucleus, in both ARC and HMC lenses. The differentially phosphorylated peptides in the lens cortex and nucleus in HMC eyes were significantly involved in the glutathione metabolism pathway. The KEGG pathway enrichment analysis indicated that the differences in phosphosignaling mediators between the ARC and HMC lenses were associated with glycolysis and the level of phosphorylated phosphoglycerate kinase 1 was lower in HMC lenses than in ARC lenses.


          We provide an overview of the differential phosphoproteomes of HMC and ARC lenses that can be used to clarify the molecular mechanisms underlying their different phenotypes.

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          Most cited references36

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          We describe a method, filter-aided sample preparation (FASP), which combines the advantages of in-gel and in-solution digestion for mass spectrometry-based proteomics. We completely solubilized the proteome in sodium dodecyl sulfate, which we then exchanged by urea on a standard filtration device. Peptides eluted after digestion on the filter were pure, allowing single-run analyses of organelles and an unprecedented depth of proteome coverage.
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            Global estimates of visual impairment: 2010.

            From the most recent data the magnitude of visual impairment and its causes in 2010 have been estimated, globally and by WHO region. The definitions of visual impairment are the current definitions of presenting vision in the International Classification of Diseases version 10. A systematic review was conducted of published and unpublished surveys from 2000 to the present. For countries without data on visual impairment, estimates were based on newly developed imputation methods that took into account country economic status as proxy. Surveys from 39 countries satisfied the inclusion criteria for this study. Globally, the number of people of all ages visually impaired is estimated to be 285 million, of whom 39 million are blind, with uncertainties of 10-20%. People 50 years and older represent 65% and 82% of visually impaired and blind, respectively. The major causes of visual impairment are uncorrected refractive errors (43%) followed by cataract (33%); the first cause of blindness is cataract (51%). This study indicates that visual impairment in 2010 is a major health issue that is unequally distributed among the WHO regions; the preventable causes are as high as 80% of the total global burden.
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              Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns.

              Reversible phosphorylation of proteins regulates the majority of all cellular processes, e.g. proliferation, differentiation, and apoptosis. A fundamental understanding of these biological processes at the molecular level requires characterization of the phosphorylated proteins. Phosphorylation is often substoichiometric, and an enrichment procedure of phosphorylated peptides derived from phosphorylated proteins is a necessary prerequisite for the characterization of such peptides by modern mass spectrometric methods. We report a highly selective enrichment procedure for phosphorylated peptides based on TiO2microcolumns and peptide loading in 2,5-dihydroxybenzoic acid (DHB). The effect of DHB was a very efficient reduction in the binding of nonphosphorylated peptides to TiO2 while retaining its high binding affinity for phosphorylated peptides. Thus, inclusion of DHB dramatically increased the selectivity of the enrichment of phosphorylated peptides by TiO2. We demonstrated that this new procedure was more selective for binding phosphorylated peptides than IMAC using MALDI mass spectrometry. In addition, we showed that LC-ESI-MSMS was biased toward monophosphorylated peptides, whereas MALDI MS was not. Other substituted aromatic carboxylic acids were also capable of specifically reducing binding of nonphosphorylated peptides, whereas phosphoric acid reduced binding of both phosphorylated and nonphosphorylated peptides. A putative mechanism for this intriguing effect is presented.

                Author and article information

                Biomed Res Int
                Biomed Res Int
                BioMed Research International
                10 May 2021
                : 2021
                : 6668845
                1Eye Institute and Department of Ophthalmology, Eye & ENT Hospital of Fudan University, Shanghai 200031, China
                2NHC Key Laboratory of Myopia (Fudan University), Key Laboratory of Myopia, Chinese Academy of Medical Sciences, Shanghai 200031, China
                3Shanghai Key Laboratory of Visual Impairment and Restoration, Shanghai 200031, China
                Author notes

                Academic Editor: Juan M. Bueno

                Author information
                Copyright © 2021 Shaohua Zhang et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                : 9 December 2020
                : 23 March 2021
                : 2 April 2021
                Funded by: Shanghai Talent Development Fund
                Award ID: 201604
                Funded by: Shanghai High Myopia Study Group
                Funded by: Shanghai Health and Family Planning Commission
                Award ID: 20184Y0014
                Funded by: National Natural Science Foundation of China
                Award ID: 81870642
                Award ID: 81970780
                Award ID: 81700819
                Award ID: 81470613
                Award ID: 81670835
                Research Article


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