Ask about this productRelated genes to: NIT2 antibody
- Gene:
- NIT2 NIH gene
- Name:
- nitrilase family member 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-12
- Date modifiied:
- 2016-10-05
Related products to: NIT2 antibody
Related articles to: NIT2 antibody
- Glutamine metabolism plays a critical role in lung cancer progression due to its substantial contribution to energy supply. NAT10 is currently the only known ac4C transferase and regulates gene expression and mRNA stability through ac4C modification, thereby influencing tumor progression. This study aimed to investigate the mechanisms by which NAT10 mediates glutamine metabolism in lung cancer. The UALCAN database was used to perform pan-cancer analysis and assess NAT10 expression in lung cancer. Cell viability, proliferation, and migration were evaluated to characterize malignant behaviors in lung cancer cells. Glutamine metabolism was assessed by measuring glutamine consumption, as well as α-ketoglutarate (α-KG) and ATP production. NAT10-associated genes were identified from the GSE3141 dataset and subjected to pathway enrichment analysis. The underlying mechanism was explored using methylated RNA immunoprecipitation and dual-luciferase reporter assays. The role of NAT10 in lung cancer progression in vivo was assessed using a xenograft model. Results showed that NAT10 was upregulated in lung cancer cells and promoted cell viability, proliferation, migration, and glutamine metabolism in A549 and H460 cells, whereas NAT10 inhibition reversed these effects. Mechanistically, NAT10 enhanced ac4C modification of NIT2 and increased NIT2 mRNA stability. Overexpression of NIT2 restored cell viability, proliferation, migration, and glutamine metabolism that were suppressed by NAT10 knockdown in A549 and H460 cells. Furthermore, inhibition of NAT10 reduced tumor growth and glutamine metabolism in nude mice. Collectively, our findings demonstrate that NAT10 promotes glutamine metabolism in lung cancer by enhancing ac4C modification of NIT2, providing new insights into the mechanisms underlying lung cancer progression. - Source: PubMed
Publication date: 2026/04/23
Yang DafuZhu YueLiu YangDai Zhaoxia - To investigate the causal relationship between mitochondrial genes and the pathogenesis of carotid plaque (CP), a multiomics-integrated Mendelian randomization (MR) analysis was performed in this study. - Source: PubMed
Publication date: 2025/11/01
Yu ZhuyuanMeng XiangyuanZong ZiyuSong QiHuo YingchaoChen Hao - Oxidative stress is a major driver of cardiovascular disease; however, the fast changes in cellular metabolism caused by short-lived reactive oxygen species (ROS) remain ill-defined. Here, we characterized changes in the endothelial cell metabolome in response to acute oxidative challenges and identified novel redox-sensitive metabolic enzymes. HO selectively increased the amount of α-ketoglutaramate (αKGM), a largely uncharacterized metabolite produced by glutamine transamination and an unrecognized intermediate of endothelial glutamine catabolism. In addition, HO impaired the catalytic activity of nitrilase-like 2 ω-amidase (NIT2), the enzyme that converts αKGM to α-ketoglutarate (αKG), by the reversible oxidation of specific cysteine residues. Moreover, a NIT2 gene variant exhibited decreased expression in humans and was associated with increased plasma αKGM concentration. Endothelial-specific knockout of NIT2 in mice increased cellular αKGM levels and impaired angiogenesis. Further, NIT2 depletion impaired endothelial cell proliferation, sprouting, and induced senescence. In conclusion, we uncover NIT2 as a redox-sensitive enzyme of the glutamine transaminase-ω-amidase pathway that acts as a metabolic switch modulating endothelial glutamine metabolism in mice and humans. - Source: PubMed
Publication date: 2025/12/17
Herrle NiklasMalacarne Pedro FWarwick TimothyCabrera-Orefice AlfredoChen YihengGheisari MaedehChatterjee SouradeepLeisegang Matthias SSarakpi TamimWionski SarahLopez MelinaKader CarineTeichmann TomDrekolia Maria-KyriakiKoch InaKeßler MarcusKlein SabineErhard Uschner FrankTrebicka JonelBrunst SteffenProschak EwgenijGünther StefanRosas-Lemus MónicaBaumgarten NinaKlatt StephanSpeer ThimoteusBibli Sofia-IrisSegarra MartaAcker-Palmer AmparoWagner Julian U GWittig IlkaDimmeler StefanieSchulz Marcel HRichards J BGilsbach RalfT Denton TravisFleming IngridHannibal LucianaBrandes Ralf PRezende Flávia - Nit1 and Nit2 were initially identified in the context of cancer research, as proteins encoded by putative (anti)oncogenes. However, the presence of homologous proteins in bacteria suggested that they might be enzymes with a fundamental metabolic function. Our group, while interacting with Arthur Cooper and his collaborators, contributed to uncovering these roles: Nit2 was identified in 2009 as an ω-amidase, the enzyme that hydrolyses the 'ω' amide of α-ketoglutaramate and α-ketosuccinamate, the 'deaminated' derivatives of glutamine and asparagine produced in some irreversible transamination reactions. Later, in 2017, we showed that Nit1 functions as a metabolite-repair enzyme. Specifically, Nit1 efficiently hydrolyzes deaminated gluthathione (dGSH), a non-functional byproduct generated by a side activity of various classical transaminases. This repair function prevents the accumulation of the useless metabolite dGSH. The physiological significance of Nit1 is underscored by recent discoveries linking its deficiency in humans to a neurological disorder. - Source: PubMed
Publication date: 2025/12/11
Van Schaftingen EmilePeracchi AlessioVeiga-da-Cunha Maria - Organic compounds such as urea and cyanate can serve as nitrogen (N) sources for nitrifying microorganisms, including ammonia-oxidizing archaea (AOA) and bacteria (AOB), complete ammonia-oxidizing (comammox) bacteria, and nitrite-oxidizing bacteria (NOB). Here we investigated metagenome-assembled genomes (MAGs) for all four nitrifier guilds generated from hydrologically variable floodplain sediments of the Wind River Basin (WRB; Riverton, WY, USA) for their genetic potential to utilize organic N compounds. A vast majority of WRB nitrifier MAGs harbored urease () and at least one urea transporter (, , ). AOA were the most abundant and phylogenetically diverse nitrifiers in WRB floodplain sediments. Several AOA MAGs encoded cyanase (), nitrilase (), omega-amidase (), nitrile hydratase (), and genes related to purine degradation, including biuret hydrolase (), oxamic transcarbamylase (), and catabolic carbamate kinase (). AOA often encoded an uncharacterized amidohydrolase collocated with , rather than allophanate hydrolase (). A small number of AOA encoded , functioning in an unknown pathway. AOB and comammox were of relatively low abundance and taxonomic diversity and were present only at certain depths in WRB; however, they encoded triuret/biuret degradation genes (, , and ), and in comammox, these genes were also collocated with . The genetic potential of ammonia oxidizers in the WRB floodplain suggests that organic N may support nitrification in this system. The proposed pathways for utilizing purine degradation products other than urea potentially expand the known metabolic capabilities of AOA, AOB, and comammox bacteria and reveal the possibility for cryptic N cycling between microbial community members. - Source: PubMed
Publication date: 2025/10/13
Rasmussen Anna NLangenfeld KatieTolar Bradley BPerzan ZachMaher KateCardarelli Emily LBargar John RBoye KristinFrancis Christopher A