ArticleMolecular vision2008
The function of filensin and phakinin in lens transparency.
Article in Molecular vision, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Participation of Lens Proteins and miRs in Traumatic and Inheritance Cataract: A Review on Diagnostic and Therapeutic Approaches for Cataract Management.Current pharmaceutical biotechnology · 2025Review
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- Article
- Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Effects of truncations in the N- and C-terminal domains of filensin on filament formation with phakinin in cell-free conditions and cultured cells.FEBS open bio · 2023Article
- Review
- Neurodegenerative Implications of Neuronal Cytoplasmic Protein Dysfunction in Response to Environmental Contaminants.Neurotoxicity research · 2021Review
- Quantitative Phosphoproteomic Comparison of Lens Proteins in Highly Myopic Cataract and Age-Related Cataract.BioMed research international · 2021Article
- Changes to Zonular Tension Alters the Subcellular Distribution of AQP5 in Regions of Influx and Efflux of Water in the Rat Lens.Investigative ophthalmology & visual science · 2020Article
- Identification of Differential Gene Expression Pattern in Lens Epithelial Cells Derived from Cataractous and Noncataractous Lenses of Shumiya Cataract Rat.BioMed research international · 2020Article
- Protective Effects of Rosmarinic Acid against Selenite-Induced Cataract and Oxidative Damage in Rats.International journal of medical sciences · 2019Article
- Localization of αA-Crystallin in Rat Retinal Müller Glial Cells and Photoreceptors.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2018Article
- The genomic basis of cichlid fish adaptation within the deepwater "twilight zone" of Lake Malawi.Evolution letters · 2017Article
- Genetic background-dependent role ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Spectral selectivity model for light transmission by the intermediate filaments in Müller cells.Journal of photochemistry and photobiology. B, Biology · 2017Article
- Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Experimental eye research · 2017Article
- The lens actin filament cytoskeleton: Diverse structures for complex functions.Experimental eye research · 2017Review
- Quantum mechanism of light transmission by the intermediate filaments in some specialized optically transparent cells.Neurophotonics · 2017Article
- Foveolar Müller Cells of the Pied Flycatcher: Morphology and Distribution of Intermediate Filaments Regarding Cell Transparency.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeBeaded filaments are lens cell-specific intermediate filaments composed of two proteins: filensin and phakinin (CP49). Filensin and phakinin are believed to function in the maintenance of lens transparency. To elucidate the function of filensin and phakinin at the molecular level, we examined the degradation of these two proteins in normal and cataractous rat lenses.
methodsA hereditary cataract model, the Shumiya cataract rat (SCR), was used for these studies. Anti-filensin antibodies were raised against three different regions of the protein, the rod domain, the inner region of the tail domain, and the outer region of the tail domain. Anti-filensin and anti-phakinin antibodies were used to examine the conformation of degradation of filensin and phakinin by western blot analysis and fluorescent immunocytochemistry of cryosectioned lenses.
resultsIn the normal lens, filensin was processed from a 94 kDa protein to proteins of 50 kDa and 38 kDa. Similarly, phakinin was processed from a 49 kDa protein to one of 40 kDa. The concentrations of filensin and phakinin in the rat lens cortex fluctuated with age and decreased during cataractogenesis. The 50 kDa form of filensin decreased significantly before opacification. In the normal lens, phakinin, the filensin rod domain, and the filensin inner tail domain localized to membrane lining regions in the shallow cortex and to the central region of the cytoplasm in the deep cortex. The COOH-terminal domain of filensin localized to the membrane lining region in the deep cortex. In pre-cataractous lenses, phakinin and the filensin rod domain localized primarily to the membranes lining the shallow cortex region and were distributed throughout the cytoplasm of lens fiber cells in the deep cortex.
conclusionsThe 50 kDa form of filensin is important for the localization of beaded filaments in lens fiber cells and for lens transparency.
Indexed as
Identifiers
18449355PMC2358922W2145643507What 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.