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Microarray analysis revealed that glutamate (show GRIN2A Proteins) cysteine ligasec overexpression and thus enhanced glutathione production has a broad impact on gene expression that largely affects different processes in young and old flies.
investigation of mutations in GCL modifier subunit and the GCL catalytic subunit that modify catalytic activity and lower glutathione levels
Neuronal overexpression of GCLc in a long-lived background extended mean and maximum life spans up to 50%, without affecting the rate of oxygen consumption by the flies
The reversibility of the dephosphorylation-dependent activation was indicated by the time-dependent inactivation of the in vitro activated Drosophila GCL, by preincubation with MgATP.
that the longevity effects of GCLc are dependent on dosage and that there are specific tissues (mushroom bodies, motor neurons, and transverse muscle cells) particularly sensitive to the benefits of GCLc overexpression.
GSH biosynthesis in the nucleus is associated with migration of only the GCLc subunit from the cytoplasm into the nucleus, and this migration requires the presence of an intact nuclear localization signal
High GCLC expression is associated with chemotherapy resistance in breast cancer.
Knockdown of CD44 (show CD44 Proteins) reduced the protein level of xCT (show SLC7A11 Proteins), a cystine transporter, and increased oxidative stress. However, an increase in GSH was also observed and was associated with enhanced chemoresistance in CD44 (show CD44 Proteins)-knockdown cells. Increased GSH was mediated by the Nrf2 (show GABPA Proteins)/AP-1 (show FOSB Proteins)-induced upregulation of GCLC, a subunit of the enzyme catalyzing GSH synthesis
GCLC polymorphisms correlated with brain GSH and Glu (show DCTN1 Proteins) levels in psychosis.
NQO1 (show NQO1 Proteins) and GCLC were both functionally sufficient to autonomously confer a tamoxifen-resistant metabolic phenotype, characterized by i) increased mitochondrial biogenesis, ii) increased ATP production and iii) reduced glutathione levels.
(i) melatonin counteracted UVR-induced alterations in the ATP synthesis and reduced free radical formation; (ii) melatonin induced the translocation of Nrf2 (show GABPA Proteins) transcription factor from the cytosol into the nucleus resulting in, (iii) melatonin enhanced gene expression of phase-2 antioxidative enzymes including gamma-glutamylcysteine synthetase (gamma-GCS), heme oxygenase-1 (HO-1 (show HMOX1 Proteins)), and NADPH (show NQO1 Proteins): quinone dehydrogenase-1 (NQO1 (show NQO1 Proteins)...
Glutaminolysis is activated in ES2 (show DGCR14 Proteins) and OVCAR3, though ES2 (show DGCR14 Proteins) exclusively synthesizes amino acids and GSH. ES2 (show DGCR14 Proteins) cells are more resistant to carboplatin than OVCAR3 and the abrogation of GSH production by BSO sensitizes ES2 (show DGCR14 Proteins) to carboplatin. HNF1beta (show HNF1B Proteins) regulates the expression of GCLC, but not GCLM (show GCLM Proteins), and consequently GSH production in ES2 (show DGCR14 Proteins)
miR-433 targets both catalytic (GCLc) and regulatory (GCLm) subunits of GCL.
Data suggest expression of hepatocyte GCLC and GCLM (show GCLM Proteins) can be regulated by dietary component; alpha-lipoic acid, a vitamin B complex nutrient, protects against oxidative stress/cytotoxicity induced by cadmium via restoration of GCLC and GCLM (show GCLM Proteins) expression.
Cigarette smoke-induced hypermethylation of the GCLC promoter is related to the initiation and progression of COPD (show ARCN1 Proteins).
GCLC and GSS (show GSS Proteins) were expressed at higher levels in colon cancer tissue, as compared with normal mucosa.
Retinal GCLC was significantly increased in rd10 (show PDE6B Proteins) mice at P21 as well as GSSG. Our results suggest alterations in retinal GCLC content and GSH and/or its precursors in these two RP animal models. Regulation of the enzymes related to GSH metabolism and the retinal concentration of glutamate (show GRIN1 Proteins) may be a possible target to delay especially cone death in Retinitis Pigmentosa
Data show that the catalytic subunit of glutamate cysteine ligase (Gclc)-derived glutathione buffers reactive oxygen species (ROS (show ROS1 Proteins)), and regulates metabolic reprogramming.
To study the biological effects of low GSH levels, we disrupted its synthesis both at birth by breeding a Gclc loxP mouse with a thy1 (show THY1 Proteins)-cre mouse and at a later age by breeding with a CaMKII (show CAMK2G Proteins)-ERT2 (show MAPK3 Proteins)-Cre (FIGSKO mouse). FIGSKO mice also develop cognitive abnormalities, i.e. learning impairment and nesting behaviors based on passive avoidance, T-Maze, and nesting behavior tests
A floxed Gclc mouse was generated and crossed with a transgenic mouse expressing Cre in the lens to generate the Lens Glutathione Synthesis Knockout mouse in which de novo GSH synthesis was completely abolished in the lens.
Clinically relevant levels of TGF-beta1 (show TGFB1 Proteins) suppresses GCLC and GCLM (show GCLM Proteins) expression in mouse lung.
Data show for the first time that GCLC may serve a dual role, as a surrogate marker for cellular redox state as well as malignant potential of melanoma cells.
The impacts of four clinical missense mutations on GCLC enzymatic function in vivo and in vitro, was evaluated.
tBHQ has beneficial effects on reducing hyperglycemia-induced kidney injury, which is associated with the enhanced expression of Nrf2 (show NFE2L2 Proteins), and its downstream antioxidant HO-1 (show HMOX1 Proteins) and gamma-GCS (show UGCG Proteins) in the glomeruli of diabetic mice
In first days of life luminescence measured was in all mice with distinct strain differences indicating NF-kappaB (show NFKB1 Proteins), superoxide dismutase (show SOD1 Proteins), gamma-glutamylcysteine synthetase, and antioxidant responsive element activity.
Hypoxia decreased 2 key enzyme activities that regulate GSH synthesis, glutamate cysteine ligase (GCL) (E.C. 184.108.40.206) and glutathione synthase (show GSS Proteins) (GS) (E.C. 220.127.116.11)
Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase is the first rate-limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. This locus encodes the catalytic subunit, while the regulatory subunit is derived from a different gene located on chromosome 1p22-p21. Mutations at this locus have been associated with hemolytic anemia due to deficiency of gamma-glutamylcysteine synthetase and susceptibility to myocardial infarction.
glutamate--cysteine ligase catalytic subunit
, glutamate-cysteine ligase, catalytic subunit
, gamma-Glutamylcysteine synthetase
, gamma-Glutamylcysteine synthetase catalytic subunit
, gamma-glutamylcysteine ligase
, glutamate cysteine ligase
, glutamate-cysteine ligase
, gamma glutamylcysteine synthetase
, glutamate--cysteine ligase, chloroplastic
, GCS heavy chain
, gamma-glutamylcysteine synthetase
, gamma GCS-HS
, gamma-glutamylcysteine synthetase heavy subunit
, Glutamylcysteine gamma synthetase light chain
, glutamate-cysteine ligase catalytic subunit