http://purl.uniprot.org/citations/33127518 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/33127518 | http://www.w3.org/2000/01/rdf-schema#comment | "AimsThe reversible protein S-glutathionylation (PSSG) modification of Fas augments apoptosis, which can be reversed by the cytosolic deglutathionylation enzyme glutaredoxin-1 (Grx1), but its roles in alcoholic liver injury remain unknown. Therefore, the objective of this study was to investigate the impact of genetic ablation of Grx1 on Fas S-glutathionylation (Fas-SSG) in regulating ethanol-induced injury.Materials and methodsWe evaluated the Grx1 activity and oxidative damage, hepatic injury related indicators, Fas-SSG, we also assess the nuclear factor-κB (NF-κB) signaling, its downstream signal, and Akt signaling cascades, Furthermore, the number of Kupffer cells and related proinflammatory cytokines between WT and Grx1-groups after alcohol exposure.Key findingsEthanol-fed mice had increased Grx1 activity and oxidative damage in the liver. Grx1-deficient mice had more serious liver damage when exposed to ethanol compared to that of wild-type mice, accompanied by increased alanine aminotransferase and aspartate aminotransferase levels, Fas-SSG, cleaved caspase-3 and hepatocyte apoptosis. Grx1 ablation resulted in the suppression of ethanol-induced NF-κB signaling, its downstream signal, and Akt signaling cascades, which are required for protection against Fas-mediated apoptosis. Accordingly, blocking NK-κB prevented Fas-induced apoptosis in WT mice but not Grx1-/-mice. Furthermore, the number of Kupffer cells and related proinflammatory cytokines, including Akt, were lower in Grx1-/-livers than those of the controls.SignificanceGrx1 is essential for adaptation to alcohol exposure-induced oxidative injury by modulating Fas-SSG and Fas-induced apoptosis."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.lfs.2020.118678"xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/author | "Guo C."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/author | "Sun X."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/author | "Ye C."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/author | "Deng Q."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/name | "Life Sci"xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/pages | "118678"xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/title | "Contribution of glutaredoxin-1 to Fas s-glutathionylation and inflammation in ethanol-induced liver injury."xsd:string |
http://purl.uniprot.org/citations/33127518 | http://purl.uniprot.org/core/volume | "264"xsd:string |
http://purl.uniprot.org/citations/33127518 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33127518 |
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