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Yoji Ueda, Melinda K. Duncan, Larry L. David; Lens Proteomics: The Accumulation of Crystallin Modifications in the Mouse Lens with Age. Invest. Ophthalmol. Vis. Sci. 2002;43(1):205-215.
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purpose. To identify modified crystallins associated with aging of lens and
produce two-dimensional electrophoresis (2-DE) proteome maps of
crystallins in mouse lens.
methods. Lens proteins from mice of increasing age or different strains were
separated by either chromatography or 2-DE. Masses of whole proteins or
tryptic peptides were analyzed by mass spectrometry. Changes in the
abundance of individual crystallins were determined by image analysis
of 2-DE gels.
results. The measured masses of all known mouse crystallins, with the exception
of γD and γF, matched the masses calculated from their reported
sequences. Analysis by 2-DE indicated that most posttranslational
modifications took place in mice after 6 weeks of age. Partially
degraded crystallins, including βB1, βB2, βB3, βA3, αA, andα
B, were found in greater proportion in the insoluble fractions.γ
-Crystallins A through F also became insoluble during aging.
However, insolubilization of γ-crystallins was associated with a
decrease in isoelectric point (pI). Aging was also associated with
increased phosphorylation of soluble αA- and αB-crystallins,
confirmed by mass measurements of these proteins eluted from 2-DE gels.
Comparison of protein profiles between several strains of mice used to
produce transgenic or knockout models of cataract indicated few
differences, except for an additional acidic form of a γ-crystallin,
possibly due to a polymorphism.
conclusions. These results suggest that partial degradation of α- andβ
-crystallins and increased acidity of γ-crystallins may cause
insolubilization during aging. The 2-DE proteome maps of mouse lens
proteins created in this study, using immobilized pH gradients, will be
useful for comparison with maps of lens proteins of mice with cataracts
so that cataract-specific modifications may be
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