BIROn - Birkbeck Institutional Research Online

    Ageing and vision: structure, stability and function of lens crystallins

    Bloemendal, H. and de Jong, W. and Jaenicke, R. and Lubsen, N.H. and Slingsby, Christine and Tardieu, A. (2004) Ageing and vision: structure, stability and function of lens crystallins. Progress in Biophysics and Molecular Biology 86 (3), pp. 407-485. ISSN 0079-6107.

    Full text not available from this repository.

    Abstract

    The α-, β- and γ-crystallins are the major protein components of the vertebrate eye lens, α-crystallin as a molecular chaperone as well as a structural protein, β- and γ-crystallins as structural proteins. For the lens to be able to retain life-long transparency in the absence of protein turnover, the crystallins must meet not only the requirement of solubility associated with high cellular concentration but that of longevity as well. For proteins, longevity is commonly assumed to be correlated with long-term retention of native structure, which in turn can be due to inherent thermodynamic stability, efficient capture and refolding of non-native protein by chaperones, or a combination of both. Understanding how the specific interactions that confer intrinsic stability of the protein fold are combined with the stabilizing effect of protein assembly, and how the non-specific interactions and associations of the assemblies enable the generation of highly concentrated solutions, is thus of importance to understand the loss of transparency of the lens with age. Post-translational modification can have a major effect on protein stability but an emerging theme of the few studies of the effect of post-translational modification of the crystallins is one of solubility and assembly. Here we review the structure, assembly, interactions, stability and post-translational modifications of the crystallins, not only in isolation but also as part of a multi-component system. The available data are discussed in the context of the establishment, the maintenance and finally, with age, the loss of transparency of the lens. Understanding the structural basis of protein stability and interactions in the healthy eye lens is the route to solve the enormous medical and economical problem of cataract.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 21 May 2019 14:46
    Last Modified: 21 May 2019 14:46
    URI: http://eprints.bbk.ac.uk/id/eprint/27613

    Statistics

    Downloads
    Activity Overview
    0Downloads
    37Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item