AADAT
- Known as:
- AADAT
- Catalog number:
- 000869A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AADAT
Related genes to: AADAT
- Gene:
- AADAT NIH gene
- Name:
- aminoadipate aminotransferase
- Previous symbol:
- -
- Synonyms:
- KATII, KAT2, KYAT2
- Chromosome:
- 4q33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-16
- Date modifiied:
- 2016-04-26
Related products to: AADAT
Related articles to: AADAT
- This study elucidated how synchronized glucose and amino acid availability regulates muscle deposition. 540 21 day-old broilers followed a 3 × 3 factorial design: AM/AP ratios (0.19, 0.29, 0.41) and SID Lys levels (1.00%, 1.20%, 1.40%). Significant interactions between AM/AP ratios and SID Lys levels on BW, BWG, breast and thigh muscle percentage, and protein deposition, 0.19 AM/AP with 1.20% SID Lys was highest, whereas 0.41 AM/AP with 1.40% SID Lys was lowest. These represented synchronized (RDS) and asynchronous (SDS) model, respectively. Compared to SDS, RDS increased serum glucose and IGF-1 levels, nutrient digestibility, and transporter expression (GLUT2, SGLT1, CAT1). Metabolomics revealed RDS optimized glycolytic and TCA flux while attenuating Lys catabolism (AASS, ALDH7A1, AADAT). Molecularly, RDS activated AKT/mTOR-mediated synthesis and suppressed AMPK/FoxO3a-mediated degradation. Collectively, synchronizing nutrients via rapidly digestible starch (0.19 AM/AP) optimizes metabolic flux and mitigates amino acid wastage, offering a critical strategy for enhancing performance in low-protein diets. - Source: PubMed
Publication date: 2026/06/29
Luo CaiweiWang JinpingGuo YumingYuan Jianmin - This study aims to evaluate serum levels of Galectin-3, Tryptophan (TRP), and kynurenine/alpha-aminoadipate aminotransferase (AADAT) in patients with rheumatoid arthritis (RA), and to investigate their potential diagnostic and prognostic implications. - Source: PubMed
Sarıyıldız LeventErbayram Fatma ZehraSivrikaya AbdullahMenevse EsmaTokak SemihAkcan Kurşun GülbenYılmaz SemaKose Hamiyet - Compared to other subtypes of breast cancer, triple-negative breast cancers (TNBC) have fewer treatment options and exhibit a worse prognosis. Through integrated transcriptomic, metabolomic, immunohistochemical, spatial, and clinical analyses, we identify the mitochondrial enzyme, α-aminoadipate aminotransferase (AADAT) as a previously unrecognized metabolic immune checkpoint in TNBC. mRNA and protein were significantly upregulated in human TNBC, and high AADAT expression was associated with reduced intra-tumoral CD8 T-cell density and inferior survival. Genetic silencing of in orthotopic murine TNBC models curtailed primary tumor growth and distant metastasis in a CD8 T-cell-dependent manner, enhanced effector T-cell activation, and sensitized tumors to dual PD-1/CTLA-4 blockade. Mechanistically, unbiased metabolomics showed increased malate levels after knockdown. Additionally, 4-hydroxyphenylpyruvate, an essential precursor for coenzyme Q(CoQ) biosynthesis, decreased following knockdown, suggesting an impaired mitochondrial electron transport chain. CoQ supplementation restored metabolic balance and reversed malate accumulation caused by knockdown, indicating that AADAT helps maintain CoQ-supported redox homeostasis, thereby preventing malate buildup and export. Notably, malate addition directly boosted CD8 T-cell oxidative metabolism, increased the NAD/NADH ratio and reactive oxygen species, and augmented TNF-α and IFN-γ production. In vivo, malate supplementation in drinking water phenocopied AADAT knockdown, restored the response to paclitaxel plus anti-PD-1 therapy in multiple independent syngeneic TNBC models with de novo or acquired resistance to immunotherapy, reduced tumor burden, and prolonged survival. In patient cohorts, higher spatially clustered intra-tumoral malate is associated with co-localization of functional CD8 T cells, decreased exhausted T-cell neighborhoods, and superior post-chemotherapy outcomes. These data position AADAT as a central metabolic orchestrator of immune escape in TNBC and nominate oral malate as a readily translatable adjuvant to reverse chemo-immunotherapy resistance in TNBC. - Source: PubMed
Publication date: 2026/01/30
Chatterjee MeghaGu FranklinSamanta SusmitaRasaily UttamThota Sai ManoharVarghese DanaQiu YunpingFordwuo Lynette Ewura EsiVillanueva HugoMcKenna Mary KathrynPark Jun HyoungZhang WeijieTian LinYu LiqunPiyarathna BadrajeeGao YangSimons Brian WesleyJung Sung YunKaranam BalasubramanyamPutluri VasantaChandandeep NagiMohamed NadaAsirvatham Jaya RuthJebakumar DeborahRao ArundatiGutierrez CarolinaOmilian Angela RMorrison CarlDas Gokul MAmbrosone ChristineSeeley Erin HKaipparettu Benny AbrahamKurland Irwin JPutluri NagireddyElkhanany AhmedDavis Andrew AZhu QianZhang Xiang H-FSreekumar Arun - Cognitive deficits from dorsolateral prefrontal cortex (dlPFC) dysfunction are common in neuroinflammatory disorders, including long-COVID, schizophrenia and Alzheimer's disease, where impairments are correlated with kynurenine inflammatory signaling. Kynurenine synthesis from tryptophan is increased under conditions of inflammation, then further metabolized to kynurenic acid (KYNA) in brain, where it blocks NMDA and α7-nicotinic receptors (nic-α7Rs). These receptors are essential for neurotransmission in dlPFC, suggesting that KYNA may contribute to higher cognitive deficits in these disorders. The current study employed several methods to examine the expression of KYNA and its synthetic enzyme, KAT II, in primate dlPFC, and to determine its effects on working memory-related dlPFC neuronal firing and cognitive functioning in aging macaques with naturally-occurring neuroinflammation. We found that KYNA, its synthetic enzyme, KAT II, and the gene encoding KAT II (AADAT), have greatly expanded expression in macaque and human dlPFC in both glia and neurons, with AADAT especially prominent in primate neurons compared to rodent PFC. In macaques, like humans, plasma kynurenine/tryptophan ratios increased with age, consistent with age-related increasing inflammation. Local application of KYNA onto dlPFC neurons markedly reduced the delay-related firing needed for working memory via actions at NMDA and nic-α7Rs, while inhibition of KAT II enhanced neuronal firing in aged macaques. Systemic administration of agents that reduce KYNA production similarly improved cognitive performance in aged monkeys. These data show that KYNA inflammatory signaling expands in primate dlPFC, and that inhibition of kynurenine-KYNA production may provide a powerful therapeutic avenue for treating higher cognitive deficits in neuroinflammatory disorders. - Source: PubMed
Yang ShengtaoDatta DibyadeepKrienen Fenna MWoo ElizabethMay AthenaAnderson George MGalvin Veronica CGonzalez-Burgos GuillermoLewis David ALing EmiMcCarroll Steven AArnsten Amy FtWang Min - Cognitive, emotional, and social impairments are pervasive across neuropsychiatric conditions, where alterations in the tryptophan (Trp)-kynurenine pathway and its product kynurenic acid (KYNA) from kynurenine aminotransferases (KATs) have been linked to Alzheimer's disease, Parkinson's disease, depression, and post-traumatic stress disorder. In novel CRISPR/Cas9-engineered KAT II knockout ( also known as ) mice, we observed despair-linked depression-like behavior with peripheral excitotoxicity and oxidative stress. KAT II's role and its crosstalk with serotonin, indole-pyruvate, and tyrosine-dopamine remain unclear. It is unknown whether deficits extend to cognitive, emotional, motor, and social domains or whether brain tissues mirror peripheral stress. - Source: PubMed
Publication date: 2025/10/31
Szabó ÁgnesGalla ZsoltSpekker EleonóraMartos DiánaSzűcs MónikaFejes-Szabó AnnamáriaFehér ÁgnesTakeda KeikoOzaki KinuyoInoue HiromiYamamoto SayoMonostori PéterToldi JózsefOno EtsuroVécsei LászlóTanaka Masaru