ArticleAge (Dordrecht, Netherlands)2011
Tight binding of proteins to membranes from older human cells.
Article in Age (Dordrecht, Netherlands), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed.
- Lipid and Cholesterol Peroxidation Leads to α-Crystallin Membrane Aggregation and Cataract Formation.Investigative ophthalmology & visual science · 2025Article
- Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging.Investigative ophthalmology & visual science · 2025Article
- Measurement of absolute abundance of crystallins in human and αA N101D transgenic mouse lenses usingExperimental eye research · 2024Article
- Interaction of βInternational journal of molecular sciences · 2023Article
- Binding of βInternational journal of molecular sciences · 2023Article
- Differences in the properties of porcine cortical and nuclear fiber cell plasma membranes revealed by saturation recovery EPR spin labeling measurements.Experimental eye research · 2021Article
- Ultrasound elastography for evaluating stiffness of the human lens nucleus with aging: a feasibility study.International journal of ophthalmology · 2021Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Noninvasive stiffness assessment of the human lens nucleus in patients with anisometropia using an ultrasound elastography system.International journal of ophthalmology · 2020Article
- Proteomics analysis and proteogenomic characterization of different physiopathological human lenses.BMC ophthalmology · 2017Article
- Small molecules, both dietary and endogenous, influence the onset of lens cataracts.Experimental eye research · 2017Review
- Analysis of proteomic differences between liquefied after-cataracts and normal lenses using two-dimensional gel electrophoresis and mass spectrometry.International journal of ophthalmology · 2017Article
- Spatially Directed Proteomics of the Human Lens Outer Cortex Reveals an Intermediate Filament Switch Associated With the Remodeling Zone.Investigative ophthalmology & visual science · 2016Article
- Quantitative proteomics analysis with iTRAQ in human lenses with nuclear cataracts of different axial lengths.Molecular vision · 2016Article
- Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Biochemistry · 2013Article
- Stable isotope dilution mass spectrometry for membrane transporter quantitation.The AAPS journal · 2013Review
- Mass spectrometry of membrane proteins: a focus on aquaporins.Biochemistry · 2013Review
- Proteomics and phosphoproteomics analysis of human lens fiber cell membranes.Investigative ophthalmology & visual science · 2013Article
- Carbon turnover in the water-soluble protein of the adult human lens.Molecular vision · 2013Article
- The LEGSKO mouse: a mouse model of age-related nuclear cataract based on genetic suppression of lens glutathione synthesis.PloS one · 2012Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The lens is an ideal model system for the study of macromolecular aging and its consequences for cellular function, since there is no turnover of lens fibre cells. To examine biochemical processes that take place in the lens and that may also occur in other long-lived cells, membranes were isolated from defined regions of human lenses that are synthesised at different times during life, and assayed for the presence of tightly bound cytosolic proteins using quantitative iTRAQ proteomics technology. A majority of lens beta crystallins and all gamma crystallins became increasingly membrane bound with age, however, the chaperone proteins alpha A and alpha B crystallin, as well as the thermally-stable protein, βB2 crystallin, did not. Other proteins such as brain-associated signal protein 1 and paralemmin 1 became less tightly bound in the older regions of the lens. It is evident that protein-membrane interactions change significantly with age. Selected proteins that were formerly cytosolic become increasingly tightly bound to cell membranes with age and are not removed even by treatment with 7 M urea. It is likely that such processes reflect polypeptide denaturation over time and the untoward binding of proteins to membranes may alter membrane properties and contribute to impairment of communication between older cells.
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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.