ArticleProceedings of the National Academy of Sciences of the United States of America1989
Visualization of crystallin droplets associated with cold cataract formation in young intact rat lens.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 36 citations in OpenAlex.
- Loss of ephrin-A5 leads to clinical signs of Peters Anomaly in a mouse model.Experimental eye research · 2026Article
- Atomistic modeling of liquid-liquid phase equilibrium explains dependence of critical temperature on γ-crystallin sequence.Communications biology · 2023Article
- Atomistic Modeling of Liquid-Liquid Phase Equilibrium Explains Dependence of Critical Temperature on γ-Crystallin Sequence.bioRxiv : the preprint server for biology · 2023Article
- Phase-Decorrelation Optical Coherence Tomography Measurement of Cold-Induced Nuclear Cataract.Translational vision science & technology · 2023Article
- Article
- Methodologies to unlock the molecular expression and cellular structure of ocular lens epithelial cells.Frontiers in cell and developmental biology · 2022Article
- Protein and Water Distribution Across Visual Axis in Mouse Lens: A Confocal Raman MicroSpectroscopic Study for Cold Cataract.Frontiers in chemistry · 2021Article
- CP49 and filensin intermediate filaments are essential for formation of cold cataract.Molecular vision · 2020Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5(-/-) mice.Experimental eye research · 2016Article
- Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Binary-liquid phase separation of lens protein solutions.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The structure, distribution, and nature of scattering elements associated with cold cataract formation in the young rat lens were studied in situ using light and electron microscopy and ImmunoGold electron microscopy. A large accumulation of spherical droplets, ranging from approximately 1.5 microns to 10 microns in diameter, were found in the lens nucleus in cold cataracts induced at 22 degrees C or 4 degrees C in TC-199 culture medium. Many droplets of all sizes were associated with the cell membranes. A cooled and then rewarmed lens was found to lose its opacity and subsequently no droplets were observed, indicating that there was a good correlation between the onset of opacification and the formation of droplets. Electron microscopy showed that droplets were composed of homogeneous electron-dense aggregates without limiting membranes. ImmunoGold study revealed that alpha-, beta-, and gamma-crystallins were all present within each droplet. This study demonstrates that extensive accumulation of the crystallin droplets in the lens nucleus is the contributing factor for the light scattering and opacification of the cold cataract in the young intact rat lens.
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