Abstract:
PURPOSE:The aim of this study was to elucidate the molecular mechanisms that lead to a dominant nuclear cataract in a mouse harboring the Y118D mutation in the alphaA-crystallin gene. METHODS:The physicochemical properties of alpha-crystallin obtained from mouse lenses with the Y118D mutation as well as a recombinant Y118D alphaA-crystallin were studied using gel filtration, two-dimensional (2D) gel electrophoresis, multi-angle light scattering, circular dichroism, fluorescence, and chaperone activities. RESULTS:Both native alpha-crystallin from mutant lens and recombinant alphaA-Y118D displayed higher molecular mass distribution than the wild-type. Circular dichroism spectra indicated changes in the secondary structures of alphaA-Y118D. The alphaA-Y118D protein prevented nonspecific protein aggregation more effectively than wild-type alphaA-crystallin. The gel filtration and 2D gel electrophoresis analysis showed a significant reduction of Y118D mutant protein in comparison with wild-type alphaA protein of heterozygous mutant lenses. Quantitative RT-PCR results confirmed a decrease in alphaA and alphaB transcripts in the homozygous mutant alpha A(Y118D/Y118D) lenses. CONCLUSIONS:The alphaA-Y118D mutant protein itself displays an increased chaperone-like activity. However, the dominant nuclear cataract is associated with a significant decrease in the amount of alphaA-crystallin, leading to a reduction in total chaperone capacity needed for maintaining lens transparency.
journal_name
Invest Ophthalmol Vis Scijournal_title
Investigative ophthalmology & visual scienceauthors
Huang Q,Ding L,Phan KB,Cheng C,Xia CH,Gong X,Horwitz Jdoi
10.1167/iovs.08-3070subject
Has Abstractpub_date
2009-06-01 00:00:00pages
2919-26issue
6eissn
0146-0404issn
1552-5783pii
iovs.08-3070journal_volume
50pub_type
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