March 2012
Volume 53, Issue 14
Free
ARVO Annual Meeting Abstract  |   March 2012
How a Mutation in the αA-Crystalline Causes Cataracts in Mice: A Molecular Explanation
Author Affiliations & Notes
  • Guido A. Zampighi
    Neurobiology, School of Optometry,
    David Geffen School Medicine/UCLA, Los Angeles, California
  • Catherine Cheng
    Neurobiology, School of Optometry,
    University of California, Berkeley, Berkeley, California
  • Xiaohua Gong
    Digestive Diseases, Vision Sci School of Optometry,
    University of California, Berkeley, Berkeley, California
  • Lorenzo Zampighi
    Digestive Diseases, Vision Sci School of Optometry,
    David Geffen School Medicine/UCLA, Los Angeles, California
  • Footnotes
    Commercial Relationships  Guido A. Zampighi, None; Catherine Cheng, None; Xiaohua Gong, None; Lorenzo Zampighi, None
  • Footnotes
    Support  EY04110 (GZ), EY021519 (XG)
Investigative Ophthalmology & Visual Science March 2012, Vol.53, 2279. doi:
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    • Get Citation

      Guido A. Zampighi, Catherine Cheng, Xiaohua Gong, Lorenzo Zampighi; How a Mutation in the αA-Crystalline Causes Cataracts in Mice: A Molecular Explanation. Invest. Ophthalmol. Vis. Sci. 2012;53(14):2279.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : To profile the 3D-distribution of the αA-crystalline in wild type controls and to determine how a single amino acid substitution (αA-Y118D) induces a dominant cataract in lenses of mice and humans.

Methods: : Thin sectioning electron microscopy was performed in lenses from: a) wild type mice labeled with anti-αA-crystalline and 2nm and 5nm diameter gold particles, b) wild type unlabeled, and c) mice carrying the αA-Y118D mutation in the absence of αB-crystalline. Tomograms calculated from conical series (55° tilts and 5° rotations) were reconstructed using the weighted back projection algorithm and refined by projection matching. Analysis of the tomograms relied on density segmentation methods based on the watershed transformation.

Results: : Reconstructions of fiber cells of wild-type mice labeled with antibody/gold particle conjugates indicated that αA-crystalline monomers or dimers decorate thin cytoskeleton filaments spaced ~7.5nm center-to-center apart. The "decorated" filaments intersected to form ~16nm diameter "bead" assemblies or larger ~32nm diameter particles. In fibers carrying the αA-Y118D mutation, the densities of "decorated" filaments and "beads" decreased steeply when normalized per unit volume of cytoplasm. In contrast, the density of larger diameter particles increased by a factor of four with respect to wild type controls. Additional changes included: a) the precipitation of soluble proteins in ordered platelets and b) the fragmentation of the plasma membrane and the communication of the fiber cytoplasm with the extra-cellular space.

Conclusions: : Analysis of the 3D-structure of fiber cells indicates that the αA-Y118D mutation changes the aggregation state of the αA-crystalline from monomers/dimers decorating thin filaments to particles comprised of larger number of subunits. In addition, other soluble crystallines formed ordered thin platelets in the fiber cytoplasm. We conclude that the αA-Y118D mutation in the αA-crystalline causes cataracts by a gain-of-order mechanism instead of the formation of light-scattering protein aggregates.

Keywords: cataract • image processing • cytoskeleton 
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