Purchase this article with an account.
Kiran Srivastava, Om P. Srivastava; Comparative 2D-Gel Crystallin Profiles of Lenses show greater Crystallin Truncation and Aggregation in Transgenic Mice Expressing αCRYAAN101D Compared to Wild-Type Mice. Invest. Ophthalmol. Vis. Sci. 2011;52(14):4745.
Download citation file:
© ARVO (1962-2015); The Authors (2016-present)
The purpose was to elucidate changes in crystallin profiles of a transgenic mouse model with deamidation of N at position 101 to D compared to wild type mice expressing WTαA.
Because relative to 5-month old WT mice with WT αA, the same aged transgenic mice with αAN101D showed cortical cataract development, the water soluble (WS)- and water insoluble(WI)-proteins from lenses of 5-month old from both type of mice were fractionated by a 2D-gel electrophoretic method and their protein profiles compared. The crystallin fragments with Mr <18 kDa and complexes >40 kDa were analyzed by mass spectrometric methods to determine their identity and post-translational modifications.
The major difference in the crystallin profiles was that lenses from transgenic mice exhibited a greater number of crystallin fragments ((53 in number) compared WT (33 in number). Similarly, crystallin complexes with (Mr>40 kDa) were more abundant in lenses of transgenic mice compared to lenses of WT mice. The mass spectrometric analysis showed that both crystallin fragments and complexes were derived from alpha-, beta- and gamma-crystallins, and these also exhibited a variety of post-translational modifications.
Increased truncations of α-, β- and γ-crystallins and formation of their complexes occurred during cataract development in the lenses of 5-month old transgenic mice compared to WT mice. These crystallin fragments and their complexes might play an important role during cataract development in the transgenic mice.
This PDF is available to Subscribers Only