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Alterations to proteins in the lens of hereditary Crygs-mutated cataractous mice
1Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai, PR China.
Purpose:
To investigate the altered expression of proteins in the lens of mice with inherited cataracts.
Methods:
Mice with inherited cataracts caused by a spontaneous mutation of the gene gamma S-crystallin (Crygs) were used as the subjects. Lens proteins were extracted and separated by two-dimensional electrophoresis (2-DE). The spots representing differential proteins were first identified by image analysis, and then further analyzed by matrix assisted laser desorption/ionization-time of flight-tandem mass spectrometry (MALDI-TOF-MS/MS).
Results:
2-DE were conducted under high (882 microg) and low dosage (190 microg) of sample. Under each condition, the numbers of protein spots found in cataract lenses were similar to those in normal lenses (p>0.05). Seventeen proteins were identified in normal lenses, including alphaA- to alphaB-, betaA1- to betaA4-, betaB1- to betaB3-, gammaA- to gammaF-, and gammaS-crystallin, and bead-filament structure protein (BFSP/filensin). Seven differential ones were consistently identified. In the cataract lenses BFSP and gammaS-crystallin were absent; gammaF-crystallin was downregulated; and betaA1-, betaB1-, betaB2-, and alphaB-crystallin were upregulated. Those abnormally upregulated crystallins, when compared to normal ones, had smaller molecular weight, suggesting possible truncation.
Conclusions:
The mutant Crygs gene can lead to changes of BFSP/filensin and other crystallins. The changes to these crystallins, together, may secondarily lead to cataract formation.
Insights
Inherited cataracts in mice result from a mutated gamma S-crystallin (Crygs) gene. This mutation alters lens proteins, including bead-filament structure protein (BFSP/filensin) and various crystallins, leading to cataract formation.
Area of Science:
- Ophthalmology
- Molecular Biology
- Genetics
Background:
- Inherited cataracts are a significant cause of vision impairment.
- Understanding the molecular mechanisms underlying cataractogenesis is crucial for developing therapeutic strategies.
Purpose of the Study:
- To investigate the altered expression of lens proteins in mice with inherited cataracts caused by a spontaneous mutation in the gamma S-crystallin (Crygs) gene.
Main Methods:
- Lens proteins were extracted from normal and cataract mice.
- Two-dimensional electrophoresis (2-DE) was used for protein separation.
- Differential protein spots were identified using matrix assisted laser desorption/ionization-time of flight-tandem mass spectrometry (MALDI-TOF-MS/MS).
Main Results:
- Seventeen proteins were identified in normal lenses, including various crystallins and bead-filament structure protein (BFSP/filensin).
- In cataract lenses, BFSP/filensin and gamma S-crystallin were absent, gamma F-crystallin was downregulated, and alpha B-, beta A1-, beta B1-, and beta B2-crystallins were upregulated.
- Upregulated crystallins showed smaller molecular weights, suggesting possible truncation.
Conclusions:
- A mutation in the gamma S-crystallin (Crygs) gene leads to significant changes in BFSP/filensin and other crystallins.
- These secondary alterations in crystallin expression are implicated in the development of inherited cataracts.
