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
- Major depressive disorder (MDD) is a complex disorder caused by genetic and environmental factors. Previous evidence implicates a potential depression subtype from interaction between childhood maltreatment (CM) and kynurenine pathway (KP) gene. Here, we investigated the top-down multi-omics KP alterations for this subtype. - Source: PubMed
Publication date: 2026/09/28
Sun YaoyaoSu MenghanKang ZheweiZhao GuoruiBai XueyingGuo JingWang YueqiLu ZheZhang YuyananFeng XiaoyangSun JunyuanYue Weihua - Fibrosis development in patients with metabolic dysfunction-associated steatotic liver disease (MASLD) is a key indicator of disease progression and clinical outcome. Bulk and single-cell transcriptomics on human tissue have advanced understanding of fibrosis progression, but interstudy heterogeneity and limited sample size hinder the identification of consistent and targetable fibrogenic mechanisms. - Source: PubMed
Publication date: 2026/09/16
Maiers Jessica LLiang TiebingGuo TingboCao ShaRamachandran PrakashRaba Teresa JRomeo StefanoJamialahmadi OveisShahrisa Etu ArmanChalasani Naga - 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