Got2
- Known as:
- Got2
- Catalog number:
- 059268A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Got2
Related genes to: Got2
- Gene:
- GOT2 NIH gene
- Name:
- glutamic-oxaloacetic transaminase 2
- Previous symbol:
- -
- Synonyms:
- mitAAT, KATIV, KAT4, KYAT4
- Chromosome:
- 16q21
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-04-26
Related products to: Got2
Related articles to: Got2
- Anoectochilus roxburghii (A. roxburghii) is a valuable herb in traditional Chinese medicine, valued for its medicinal properties. Wild A. roxburghii is rare and requires specific environmental conditions, making artificial cultivation challenging. High-temperature acclimation in plants - physiological and biochemical adjustments to tolerate elevated temperatures - has practical applications in agriculture. Our previous study showed that high-temperature acclimation enhances the heat tolerance of the A. roxburghii accession 'Meihuashan', though the molecular basis remains unclear. In this study, we conducted transcriptomic and metabolomic analyses on control (CK), 3-day high-temperature acclimated (T1, 35°C), and 4-day high-temperature acclimated (T2, 35°C) 'Meihuashan' plants. RNA sequencing identified 79,086 unigenes and 12,404 protein-coding genes. Gene ontology and pathway enrichment analyses revealed that metabolic pathways were significantly enriched in the high-temperature response. Subsequent untargeted metabolomic analysis detected 1014 metabolites in the high-temperature treatment group, with 157 differentially expressed metabolites. Orthogonal partial least square-discriminant analysis revealed differentially expressed metabolites associated with flavone, phenylpropanoid, and alkaloid biosynthesis, along with amino acid, lipid, and carbohydrate metabolism. Integrated analysis further highlighted the central role of the carbon fixation pathway, in which key enzyme-encoding genes (e.g. PCK1, GOT2, ALDOA, TPI1) and their corresponding metabolites exhibited significant co-variation under high-temperature stress. These findings suggest that metabolic changes involving amino acids, lipids, and carbohydrates may play a key role in the high-temperature acclimation of 'Meihuashan'. - Source: PubMed
Zhang ShuheLi HaimingZou HuiLi HepingLin JiangboDai Yimin - Photoreceptor (PR) loss causes vision loss in many blinding diseases, and effective therapies to prevent this cell loss are lacking. Aspartate aminotransferases (GOTs), located in the cytosol (GOT1) and mitochondria (GOT2), are key components of the malate-aspartate shuttle, which transfers reducing equivalents from cytosol to mitochondria. Previous work has implicated the GOTs as potential modulators of blinding retinal disease. To determine the roles of GOT1 and GOT2 in rod PRs, we generated rod PR-specific or conditional knockout mice ( or cKO). We previously showed that cKO causes PR degeneration and is accompanied by NADH accumulation and a decreased retinal NAD /NADH ratio. Here, we show that NADH oxidation via metabolic or genetic means prolongs PR survival in cKO animals, implicating NADH accumulation, or reductive stress, as a key driver of PR degeneration. In contrast, cKO causes minimal PR degeneration and alterations in retinal NADH and the NAD /NADH ratio that oppose reductive stress. Interestingly, GOT2, but not GOT1, is decreased in multiple models of PR degeneration, including retinal detachment (RD) where the NAD /NADH ratio favors a reductive state. Notably, loss of in PRs demonstrates a neuroprotective effect after experimental RD suggesting decreased GOT2 expression may be part of a stress response to promote PR survival. Overall, this study illustrates the differential dependence on the GOTs for PR health, provides evidence that an overly reductive environment is detrimental to PR survival, and identifies GOT2 as a novel therapeutic target with potentially broad application in blinding diseases. - Source: PubMed
Publication date: 2026/04/07
Chen MeiniWeh EricGoswami Moloy TWeh Katherine MHager HeatherSajjakulnukit PeterWeingarten AviSubramanya ShubhaMiller NicholasChaudhury SraboniPiraino EmmaChandel Navdeep SRyals Renee CLyssiotis Costas AWubben Thomas J - Glucose is an important fuel in cancer cells, however, its availability may be limited in solid tumors. Cell-autonomous, metabolic adaptations of cancer cells and non-malignant cells to glucose deprivation are still incompletely understood. - Source: PubMed
Publication date: 2026/03/03
Konrad BarbaraBluemel GabrieleHaitzmann TheresaFrech TobiasVandekeere AnkePlanque MélanieBubalo VisnjaSchindlmaier KatharinaJäger VanessaDengler Michael AStryeck SarahBrcic LukaLindenmann JörgStiegler PhilippBresilla DoruntinaMadreiter-Sokolowski Corina TMadl TobiasEichmann Thomas OKneidinger NikolausFendt Sarah-MariaLeithner Katharina - The malate-aspartate shuttle is a major electron shuttle that transfers reducing equivalents from the cytosol to the mitochondria, where they can be safely deposited onto the electron transport chain. Nevertheless, many proliferating cells discard reducing equivalents in the form of lactate, raising the question of what factors limit electron shuttle use. Here, we show that aspartate availability determines engagement of the malate-aspartate shuttle. In proliferating cells, increasing aspartate availability enhances use of the malate-aspartate shuttle and increases metabolism of glucose-derived pyruvate in mitochondria, a process that requires regeneration of oxidized electron carriers in the cytosol. During differentiation, elevated flux through the malate-aspartate shuttle cells enables cells to fuel mitochondrial networks from glucose-derived carbon. Engineering aspartate demand reverses this metabolic signature of differentiated cells. Together, these results demonstrate that cell-state-specific demand for aspartate is sufficient to determine use of the malate-aspartate shuttle and drives changing mitochondrial substrate preferences during differentiation. - Source: PubMed
Publication date: 2026/02/26
Brunner Julia SBridgeman Anna EJackson Benjamin TChakraborty SangitaFagoaga-Eugui MaiderParas Katrina IXie AbigailArnold Paige KLosner JuliaFinley Lydia W S - Diet-phytochemical derived activation, host and microbial tryptophan metabolism represent the dominant route to endogenously mediated stimulation of physiological Ah receptor (AHR) activity. Whether host tryptophan metabolism provides a phytochemical independent circadian AHR tone has not been established. Using mice maintained on a nocturnally restricted feeding schedule with a nutritionally defined diet, we utilized quantitative gene/protein expression analyses in conjunction with targeted metabolomics to examine the temporal relationship between host tryptophan metabolism and circadian AHR activity. Time-resolved, targeted LCMS metabolomic, gene, and protein expression analyses reveal circadian cycling of hepatic tryptophan metabolizing enzymes (TDO2, TAT, GOT1, GOT2, KAT1, KAT2, and IL4I1) and serum tryptophan metabolites (indole-3-acetate, indole-3-lactate, indole-3-propionate, indole aldehyde, kynurenine, kynurenic acid) previously established as AHR ligands. We observed cyclical hepatic AHR activity directed by circadian feeding. These data suggest that a circadian rhythm of tryptophan metabolism orchestrates a daily tone in AHR activity that likely modulates AHR dependent physiology. - Source: PubMed
Publication date: 2026/01/12
Morgan Ethan WMurray Iain ACoslo Denise MPatterson Andrew DPerdew Gary H