@article{10.1167/iovs.10-5302,
    author = {Stella, David R. and Floyd, Kyle A. and Grey, Angus C. and Renfrow, Matthew B. and Schey, Kevin L. and Barnes, Stephen},
    title = "{Tissue Localization and Solubilities of αA-crystallin and its Numerous C-terminal Truncation Products in Pre- and Postcataractous ICR/f Rat Lenses}",
    journal = {Investigative Ophthalmology & Visual Science},
    volume = {51},
    number = {10},
    pages = {5153-5161},
    year = {2010},
    month = {10},
    abstract = "{   To investigate the tissue distribution and solubilities of various αA-crystallin truncation products in the cataractous ICR/f rat model.    Rat 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.    Ten 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.    A 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.  }",
    issn = {1552-5783},
    doi = {10.1167/iovs.10-5302},
    url = {https://doi.org/10.1167/iovs.10-5302},
    eprint = {https://arvojournals.org/arvo/content\_public/journal/iovs/932962/z7g01010005153.pdf},
}