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GSTM3
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==Publications== {{medline-entry |title=Age-associated changes in GSH S-transferase gene/proteins in livers of rats. |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/30444463 |abstract=Glutathione S-transferases (GSTs) are phase-II metabolic enzymes playing important roles in drug metabolism, anti-oxidative stress and anti-aging. Age is a key factor influencing GSTs expression. Thus, age-related changes of 10 GSTs were examined. Livers from male Sprague-Dawley rats at fetus (-2 d), neonates (1, 7, 14 and 21 d), puberty (28 and 35 d), adulthood (60 and 180 d), and aging (540 and 800 d), were collected and subjected to qPCR analysis. Liver proteins from 14, 28, 60, 180, 540 and 800 d were also extracted for selected protein analysis by Western-blot. The expression of [[GSTA1]] and [[GSTP1]] increased over the life span and the expression of [[GSTA4]], [[GSTO1]] and [[GSTZ1]] gradually increased until adulthood, and slightly decreased at 800 days. The expression of [[GSTM1]], [[GSTM3]], [[GSTT1]], [[GSTT2]] and [[GSTK1]] gradually increased until adulthood, but significantly decreased during aging of 540 and 800 days. There is a small peak at 7-14 d for [[GSTA1]], [[GSTP1]] and [[GSTZ1]]. The protein expression of [[GSTA1]], [[GSTM1]] and [[GSTP1]] followed the trend of mRNA changes. This study characterized three expression patterns of 10 GSTs during development and aging in rat liver, adding to our understanding of anti-aging role of GSTs. |mesh-terms=* Aging * Animals * Glutathione S-Transferase pi * Glutathione Transferase * Isoenzymes * Liver * Male * Rats * Rats, Sprague-Dawley |keywords=* Ontogeny * aging * glutathione S-transferases * rat liver |full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6748684 }} {{medline-entry |title=Relationship Between the Altered Expression and Epigenetics of [[GSTM3]] and Age-Related Cataract. |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27607418 |abstract=Glutathione S-Transferase Mu 3 ([[GSTM3]]) protects the lens from oxidative stress that contributes to age-related cataract ([[ARC]]) formation. We examined the expression and epigenetics of [[GSTM3]] in lens epithelial cells (LECs) and lens cortex of [[ARC]], and investigated the potential role of molecular changes in [[ARC]] pathogenesis. This study included 120 [[ARC]]s and 40 controls. Expression of [[GSTM3]], DNA methylation, and histone modification were assessed by quantificational real-time PCR, Western blot, bisulfite-sequencing PCR, pyrosequencing, and chromatin immunoprecipitation assay. Human lens epithelial (HLE) cell lines, SRA01/04 and HLEB3, were served as an in vitro model to observe the relationship between epigenetic status and [[GSTM3]] expression. Potential transcription factors binding to [[GSTM3]] promoter were detected by electrophoretic mobility shift assay. Expression of [[GSTM3]] decreased in [[ARC]] lens tissues compared to that in the controls, which correlated with the hypermethylation of [[GSTM3]] promoter. Lower level of [[GSTM3]] was detected in HLEB3 than in SRA01/04, while HLEB3 displayed hypermethylation of [[GSTM3]] and SRA01/04 did not. Compared to SRA01/04, HLEB3 displayed lower acetylated H3 and higher trimethylated H3K9 levels. After treatment with DNA methyltransferase inhibitor or histone deacetylase inhibitor, HLEB3 had an increased [[GSTM3]] expression. Methylation of [[GSTM3]] promoter abrogated the potential transcription factor binding. The [[GSTM3]] expression declined in hydrogen peroxide-treated HLE cell lines. Expression of [[GSTM3]] might be regulated by epigenetic changes in lens tissue. Hypermethylation in [[GSTM3]] promoter and altered histone modification might have a role in the [[ARC]] formation. The results provided a potential strategy of [[ARC]] management by manipulating epigenetic changes. |mesh-terms=* Aging * Cataract * Cells, Cultured * DNA * DNA Methylation * Epigenomics * Female * Gene Expression Regulation * Glutathione Transferase * Humans * Lens Cortex, Crystalline * Male * Middle Aged * Oxidative Stress * Promoter Regions, Genetic * Real-Time Polymerase Chain Reaction |full-text-url=https://sci-hub.do/10.1167/iovs.16-19242 }}
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