Dataset Information

An increase in phosphorylation and truncation of crystallin with the progression of cataracts.

ABSTRACT:

Background

Cataracts are the leading cause of blindness worldwide; however, there is no evidence regarding the direct formation of cataracts. At present, there is no treatment method other than surgery to prevent the formation or progression of cataracts.

Objective

Understanding the protein changes during various stages of cataracts might help realize the mechanism of the formation and progression of cataracts.

Methods

Lens materials were collected from cataract surgery. Cataracts were classified according to lens opacity using the gradation of the Lens Opacities Classification System. Lens proteins were separated by 2-dimensional polyacrylamide gel electrophoresis. Protein spots were visualized by Coomassie blue staining, and expression patterns were analyzed. Protein spots of interest were excised from 2-dimensional polyacrylamide gel electrophoresis gels, digested in situ with trypsin, and analyzed by mass spectrometry and liquid chromatographic tandem mass spectrometry.

Results

Crystallin was the major protein in the cataract lens, and αA, βB1, αB, and βA4 were the dominant types. Crystallin αB and βA4 increased with the formation of lens opacity. Moreover, phosphorylation and truncation of these proteins increased with the progression of cataracts.

Conclusion

Crystallin αB and βA4 and phosphorylation and truncation of crystallin in the lens might contribute to the formation of cataracts. In contrast, acetylation was not dominant in the progression of cataracts and did not play major role in the formation of cataracts.

SUBMITTER: Lin HJ

PROVIDER: S-EPMC3862202 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature

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Publications

An increase in phosphorylation and truncation of crystallin with the progression of cataracts.

Lin Hui-Ju HJ Lai Chien-Chen CC Huang Shiuan-Yi SY Hsu Wei-Yi WY Tsai Fuu-Jen FJ

Current therapeutic research, clinical and experimental 20130601

<h4>Background</h4>Cataracts are the leading cause of blindness worldwide; however, there is no evidence regarding the direct formation of cataracts. At present, there is no treatment method other than surgery to prevent the formation or progression of cataracts.<h4>Objective</h4>Understanding the protein changes during various stages of cataracts might help realize the mechanism of the formation and progression of cataracts.<h4>Methods</h4>Lens materials were collected from cataract surgery. Ca ...[more]

PMID: 24384929

Similar Datasets

Project description:Purpose:To identify mutations in crystallin genes in Chinese families with congenital cataracts. Methods:Forty-two unrelated families with non-syndromic congenital cataracts were enrolled in this study. The coding exons and adjacent intronic regions of crystallin genes, including CRYAA, CRYAB, CRYBA1, CRYBA4, CRYBB1, CRYBB2, CRYBB3, CRYGC, CRYGD and CRYGS, were analyzed with Sanger sequencing. Novel variants were further evaluated in 112 ethnically matched controls. To confirm the novel mutations, short tandem repeat (STR) haplotypes were constructed to check the cosegregation with congenital cataract. The pathogenic potential of the novel mutations were assessed using bioinformatics tools, including Sorting Intolerant From Tolerant v5.1.1 (SIFT), Polymorphism Phenotyping v2 (PolyPhen-2), and Human Splicing Finder. The pathogenicity of all the mutations was evaluated according to the guidelines of the American College of Medical Genetics (ACMG) and InterVar software. Results:Seven previously reported mutations in crystallin genes identified in ten unrelated families were associated with the congenital nuclear cataracts. Four novel mutations in crystallin genes, including c.35G>T (p.R12L) in CRYAA, c.463C>A (p.Q155K) in CRYBB2, IVS1 c.10-1G>A in CRYGC, and c.346delT (p.F116Sfsx29) in CRYGD, were identified in four unrelated families with congenital cataracts. These mutations cosegregated with all affected individuals in each family were not observed in the unaffected family members or in the 112 unrelated controls. All four novel mutations were categorized as disease "likely pathogenic" except IVS1 c.10-1G>A in CRYGC "pathogenic" using InterVar software in accordance with the ACMG standard. Mutations in crystallin genes were responsible for 33.33% of the Chinese families with congenital cataracts in this cohort. Conclusions:In this study, we identified four novel mutations in crystallin genes in Chinese families with congenital cataracts. The results expand the mutational spectrum of crystallin genes, which may be helpful for the molecular diagnosis of congenital cataracts in the era of precision medicine.

Dataset Information

An increase in phosphorylation and truncation of crystallin with the progression of cataracts.

Background

Objective

Methods

Results

Conclusion

Publications

An increase in phosphorylation and truncation of crystallin with the progression of cataracts.

Similar Datasets

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