ArticleMolecular vision2011
Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lenses.
Article in Molecular vision, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- Emerging Trends and Research Foci in Cataract Genes: A Bibliometric and Visualized Study.Frontiers in genetics · 2021Pooled it
- Review
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- Identification of CryAB as a target of NUAK kinase activity in Drosophila muscle tissue.Genetics · 2023Article
- Proteomic characterization of the human lens and Cataractogenesis.Expert review of proteomics · 2021Review
- Quantitative Phosphoproteomic Comparison of Lens Proteins in Highly Myopic Cataract and Age-Related Cataract.BioMed research international · 2021Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- The Human Eye Proteome Project: Updates on an Emerging Proteome.Proteomics · 2018Review
- High-throughput sequencing reveals novel lincRNA in age-related cataract.International journal of molecular medicine · 2017Article
- Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Cellular and molecular life sciences : CMLS · 2015Review
- Clinical proteomics identifies urinary CD14 as a potential biomarker for diagnosis of stable coronary artery disease.PloS one · 2015Article
- Human protein aging: modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates.Aging cell · 2014Article
- Clinical proteomics identifies potential biomarkers in Helicobacter pylori for gastrointestinal diseases.World journal of gastroenterology · 2014Review
- Crybb2 coding for βB2-crystallin affects sensorimotor gating and hippocampal function.Mammalian genome : official journal of the International Mammalian Genome Society · 2013Article
- Review
- Proteomics and phosphoproteomics analysis of human lens fiber cell membranes.Investigative ophthalmology & visual science · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposePost-translational modification (PTM) of lens proteins is believed to play various roles in age-related lens function and development. Among the different types of PTM, phosphorylation is most noteworthy to play a major role in the regulation of various biosignaling pathways in relation to metabolic processes and cellular functions. The present study reported the quantitative analysis of the in vivo phosphoproteomics profiles of human normal and cataractous lenses with the aim of identifying specific phosphorylation sites which may provide insights into the physiologic significance of phosphorylation in relation to cataract formation.
methodsTo improve detection sensitivity of low abundant proteins, we first adopted SDS-gel electrophoresis fractionation of lens extracts to identify and compare the protein compositions between normal and cataractous lenses, followed by tryptic digestion, enrichment of phosphopeptides by immobilized metal affinity chromatography (IMAC) and nano-liquid chromatography coupled tandem mass spectrometry (nanoLC-MS/MS) analysis.
resultsBy comprehensively screening of the phosphoproteome in normal and cataractous lenses, we identified 32 phosphoproteins and 73 phosphorylated sites. The most abundantly phosphorylated proteins are two subunits of β-crystallin, i.e., βB1-crystallin (12%) and βB2-crystallin (12%). Moreover, serine was found to be the most abundantly phosphorylated residue (72%) in comparison with threonine (24%) and tyrosine (4%) in the lens phosphoproteome. The quantitative analysis revealed significant and distinct changes of 19 phosphoproteins corresponding to 28 phosphorylated sites between these two types of human lenses, including 20 newly discovered novel phosphorylation sites on lens proteins.
conclusionsThe shotgun phosphoproteomics approach to characterize protein phosphorylation may be adapted and extended to the comprehensive analysis of other types of post-translational modification of lens proteins in vivo. The identification of these novel phosphorylation sites in lens proteins that showed differential expression in the cataractous lens may bear some unknown physiologic significance and provide insights into phosphorylation-related human eye diseases, which warrant further investigation in the future.
Indexed as
Identifiers
21264232PMC3025096W1489619761What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.