Project description:To understand the global view of dysregulated genes and pathwyas in CRYAAN101D lenses, RNA sequencing of 2 & 4 months old CRYAAWT and CRYAAN101D lenses was carried out.

2014-05-28 | GSE57959 | GEO

Comparison of expression data of 2 & 4- months old CRYAAN101D versus CRYAAWT lenses

Project description:To understand the global view of dysregulated genes and pathwyas in CRYAAN101D lenses, RNA sequencing of 2 & 4 months old CRYAAWT and CRYAAN101D lenses was carried out. Determination of differential gene expression between CRYAAWT and CRYAAN101D in 2 & 4 months old lenses

2014-05-28 | E-GEOD-57959 | biostudies-arrayexpress

Microarray data of ICR lenses at each week of age

Project description:Analysis of gene expression changes during cataract progression.

2023-10-26 | GSE230320 | GEO

Expression data from Sprague Dawley rat lenses cultured for 4 days - addition of various inhibitors

Project description:We created a rat sugar cataract model and examined the effects of various inhibitors on lens clouding. Lenses were removed from 6-week-old SD rats and cultured in M199 medium containing 30 mM galactose.

2020-03-04 | GSE135000 | GEO

Microarray data of ICR lenses

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-10-26 | GSE230323 | GEO

Expression data from renal cortex of ICR-derived Glomerulonephritis (ICGN) mice and ICR mice

Project description:ICR-derived glomerulonephritis (ICGN) mice is a novel inbred strain of mice with a hereditary nephrotic syndrome. Deletion mutation of tensin 2 (Tns2), a focal adhesion molecule, has been suggested to be responsible for nephrotic syndrome in ICGN mice, however, existence of other associative factors has been suggested. To identify additional associative factors and to better understand onset mechanism of nephrotic syndrome in ICGN mice, comprehensive gene expression analysis using DNA microarray was conducted. Immune-related pathways were markedly altered in ICGN mice kidney as compared with ICR mice. Furthermore, gene expression level of complement component 1, s subcomponent (C1s), whose human homologue has been reported to associate with lupus nephritis, was markedly low in ICGN mice kidney. RNA from renal cortex of 4- and 8-week-old ICGN and ICR mice was extracted and processed for hybridization on Affymetrix microarrays (N=3).

2013-07-31 | E-GEOD-45005 | biostudies-arrayexpress

Dehydroalanine and Dehydrobutyrine in Aging and Cataractous Lenses

Project description:Protein post-translational modifications (PTMs) have been associated with aging and age-related diseases. PTMs are particularly impactful in long-lived proteins, such as those found in the ocular lens, because they accumulate with age. Two post-translational modifications that lead to protein-protein crosslinks in aged and cataractous lenses are dehydroalanine (DHA) and dehydrobutyrine (DHB); formed from cysteine/serine and threonine residues, respectively. The purpose of this study was to quantitate DHA and DHB in human lens proteins as a function of age and cataract status. Human lenses of various ages were divided into five donor groups: transparent lenses (18–22-year-old, 48–64-year-old, and 70–93-year-old) and cataractous human lenses of two age groups (48–64-year-old lenses, and 70–93-year-old lenses) and were subjected to proteomic analysis. Relative DHA and DHB peptide levels were quantified and compared to their non-modified peptide counterparts. For most lens proteins containing DHA or DHB, higher amounts of DHA- and DHB-modified peptides were detected in aged and cataractous lenses. DHA-containing peptides were classified into three groups based on abundance changes with age and cataract: those that (1) increased only in age-related nuclear cataract (ARNC), (2) increased in aged and cataractous lenses, and (3) decreased in aged lenses and ARNC. There was no indication that DHA or DHB levels were dependent on lens region. In most donor groups, proteins with DHA and DHB were more likely to be found among urea-insoluble proteins rather than among water- or urea-soluble proteins. DHA and DHB formation may induce structural effects that make proteins less soluble in water that leads to age-related protein insolubility and possibly aggregation and light scattering.

2023-10-12 | PXD045734 | Pride

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