ArticleInvestigative ophthalmology & visual science2010
Tissue localization and solubilities of αA-crystallin and its numerous C-terminal truncation products in pre- and postcataractous ICR/f rat lenses.
Article in Investigative ophthalmology & visual science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Gene profiles and mutations in the development of cataracts in the ICR rat model of hereditary cataracts.Scientific reports · 2023Article
- Spatially Resolved Proteomics Reveals Lens Suture-Related Cell-Cell Junctional Protein Distributions.Investigative ophthalmology & visual science · 2023Article
- High-Resolution Imaging Mass Spectrometry of Human Donor Eye: Photoreceptors Cells and Basal Laminar Deposit of Age-Related Macular Degeneration.Advances in experimental medicine and biology · 2023Article
- Lipid Landscape of the Human Retina and Supporting Tissues Revealed by High-Resolution Imaging Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2020Article
- Localization of the lens intermediate filament switch by imaging mass spectrometry.Experimental eye research · 2020Article
- MALDI imaging mass spectrometry of β- and γ-crystallins in the ocular lens.Journal of mass spectrometry : JMS · 2020Article
- Bis(monoacylglycero)phosphate lipids in the retinal pigment epithelium implicate lysosomal/endosomal dysfunction in a model of Stargardt disease and human retinas.Scientific reports · 2017Article
- Small molecules, both dietary and endogenous, influence the onset of lens cataracts.Experimental eye research · 2017Review
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
- High spatial resolution imaging mass spectrometry of human optic nerve lipids and proteins.Journal of the American Society for Mass Spectrometry · 2015Article
- A method to prevent protein delocalization in imaging mass spectrometry of non-adherent tissues: application to small vertebrate lens imaging.Analytical and bioanalytical chemistry · 2015Article
- Lens crystallin modifications and cataract in transgenic mice overexpressing acylpeptide hydrolase.The Journal of biological chemistry · 2014Article
- Top-down proteomics with mass spectrometry imaging: a pilot study towards discovery of biomarkers for neurodevelopmental disorders.PloS one · 2014Article
- Analysis of tissue specimens by matrix-assisted laser desorption/ionization imaging mass spectrometry in biological and clinical research.Chemical reviews · 2013Review
- Patterns of gene expression in microarrays and expressed sequence tags from normal and cataractous lenses.Human genomics · 2012Article
- Oligomerization with wt αA- and αB-crystallins reduces proteasome-mediated degradation of C-terminally truncated αA-crystallin.Investigative ophthalmology & visual science · 2012Article
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6 authors.
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Abstract
purposeTo investigate the tissue distribution and solubilities of various αA-crystallin truncation products in the cataractous ICR/f rat model.
methodsRat lenses from precataractous (21-day) and postcataractous (100-day) ICR/f rats were sectioned and applied to a matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) target plate. Mass spectrometry images were collected to obtain a macromolecular profile of the abundant lens proteins. Separately, age-matched lenses were extracted into water-soluble (WS) and water-insoluble/urea-soluble (WI-US) fractions and subjected to MALDI-TOF mass spectrometry to correlate the protein solubilities with the imaging data. Protein identities were assigned by using a top-down proteomics approach on a high-resolution mass spectrometer.
resultsTen novel αA-crystallin truncation products were identified, along with six previously known αA-crystallin truncation products. Nearly all truncations exhibited nuclear localization, with larger truncated products displaying a ringlike localization that progressed outward toward the extranuclear, cortical region. The distributions were similar in both ages with the only significant difference being the amount of tissue area encompassed by a particular species with increasing age. Almost all nuclear products fractionated into the WI-US fraction, whereas the five largest extranuclear species exhibited mixed solubility.
conclusionsA successful methodology for the sectioning and imaging of pre- and postcataractous ICR/f rat lenses has been established. Data collected from these analyses indicate that there are multiple αA-crystallin truncation products present in both pre- and postcataractous rats. Furthermore, these species have defined lenticular localizations and unique solubilities that may be a consequence of lens development and protein function within the lens environment.
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