The C Terminus of Lens Aquaporin 0 Interacts with the Cytoskeletal Proteins Filensin and CP49

Kristie M Lindsey Rose, Robert G. Gourdie, Alan R. Prescott, Roy A. Quinlan, Rosalie K. Crouch, Kevin L. Schey (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    67 Citations (Scopus)

    Abstract

    PURPOSE. Aquaporin 0 (AQP0), the most abundant membrane protein in the lens, is a water-permeable channel, has a role in fiber cell adhesion, and is essential for fiber cell structure and organization. The purpose of this study was to identify proteins that interact with the C terminus of AQP0, by using a proteomics approach, and thus further elucidate the role of AQP0 in the human lens. METHODS. AQP0 C-terminal peptides and AQP0 antibody affinity chromatography were used for affinity purification of interacting human lens proteins. Purified proteins were digested with trypsin, analyzed by liquid chromatography (LC)-tandem mass spectrometry and identified after database searching and manual examination of the mass spectral data. Colocalization of AQP0 with filensin and CP49, two proteins identified after mass spectrometric analysis, were examined by immunoconfocal and immunoelectron microscopy of lens sections. RESULTS. The proteomics approach used to identify affinity-purified proteins revealed the lens-specific intermediate filament proteins filensin and CP49. With immunoconfocal microscopy, regions of colocalization of AQP0 with filensin and CP49 at the fiber cell plasma membrane in the lens cortex were defined. Immunoelectron microscopy confirmed that filensin and AQP0 were present in the same membrane compartments. CONCLUSIONS. These studies suggest a novel interaction between an aquaporin water channel and intermediate filaments, an interaction through which AQP0 may maintain lens fiber cell shape and organization.

    Original languageEnglish
    Pages (from-to)1562-1570
    Number of pages9
    JournalInvestigative Ophthalmology and Visual Science
    Volume47
    Issue number4
    DOIs
    Publication statusPublished - Apr 2006

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