Ask about this productRelated genes to: Bcat1 Blocking Peptide
- Gene:
- BCAT1 NIH gene
- Name:
- branched chain amino acid transaminase 1
- Previous symbol:
- BCT1
- Synonyms:
- -
- Chromosome:
- 12p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-03-07
Related products to: Bcat1 Blocking Peptide
Related articles to: Bcat1 Blocking Peptide
- Hypoxia is a common characteristic of solid tumors, especially in hepatocellular carcinoma (HCC). Hypoxia-inducible factors (HIFs), particularly HIF-1α, mediate metabolic adaptation, which is crucial for survival of hypoxic cells. Branched-chain amino transferase 1 (BCAT1) catalyzes the reversible transamination reaction between branched-chain amino acids (BCAAs) and branched-chain keto acids (BCKAs), involving the inter-conversion of α-ketoglutarate (α-KG) and glutamate. We investigate and delineate the mechanisms by which BCAT1 consumes α-KG and stabilizes HIF-1α, suppressing α-KG-dependent oxygen dehydrogenase, prolyl hydroxylase-domain protein (PHD), inducing HIF-1α-mediated metabolic reprogramming and promoting hypoxic survival of HCC. We evaluate the potency of a BCAT1 inhibitor, ERG245, as a single or combination treatment with tyrosine kinase inhibitor (TKI) in vivo. We further validate the over-expression and correlation of BCAT1 and HIF-1α downstream metabolic genes in HCC clinical samples. Our results indicate that BCAT1 benefits HCC growth through HIF-1α-induced metabolic reprogramming. Targeting BCAT1 will provide an effective therapeutic strategy for HCC patients. - Source: PubMed
Publication date: 2026/04/29
Zhang Misty ShuoKwan Kenneth Kin-LeungTse Aki Pui-WahWang GengchaoWei Larry LaiSun KejieChui Noreen Nog-QinLee DerekBao Macus Hao-RanPang XiaoxuanWu ZhenqiChen YanyanWang YangyangYang ZifanJiang XueLi QidongZhang YanZhong YajieCheu Jacinth Wing-SumChen YilingLi WeixingWong Chun-MingWang JianingCai ZongweiZhang QiLiang TingboNg Irene Oi-LinPapathanassiu Adonia EWong Carmen Chak-Lui - Glucagon activates amino acid catabolism and gluconeogenesis in adults. Elevated glucagon concentrations in the fetus occur in pregnancy complications, such as fetal growth restriction (FGR) and hypoxia, yet the impact of chronic fetal hyperglucagonemia is unknown. Using chronically catheterized pregnant sheep, glucose tracers, and liver tissue biopsies, we investigated the effects of nine days of glucagon infusion at 5 or 50 ng/kg/min in late-gestation fetal sheep that increased plasma glucagon concentrations by 800%. Glucagon-infused fetuses were euglycemic and exhibited lower plasma and hepatic amino acid concentrations. They also had increased hepatic mRNA expression of amino acid catabolism genes, including ARG2, GLS2, BCAT1, BCAT2, GLUL, HAL, UROC1, and PPARGC1A. Metabolite profiling in liver tissue revealed enrichment of pathways associated with amino acid degradation, elevated tri- and diphosphate nucleotides, and changes in fatty acid metabolites, supporting enhanced hepatic energy metabolism from amino acid oxidation. Hepatic glycogen content was reduced in glucagon-infused fetuses and the gluconeogenic genes PCK1 and G6PC1 were increased, although fetal glucose production was not detected. These findings demonstrate that in the fetal liver, chronic hyperglucagonemia activates amino acid catabolic pathways, indicating a physiological role for glucagon in regulating fetal amino acid homeostasis. These findings have implications for understanding fetal hepatic adaptations during chronic fetal hyperglucagonemia that can occur in the setting of FGR or hypoxia. - Source: PubMed
Publication date: 2026/04/28
Tanner Amelia RCilvik Sarah NNguyen Marjorie ABrown Laura DAnthony Russell VWright Clyde JWesolowski Stephanie RRozance Paul J - Metabolic diseases such as obesity, type 2 diabetes mellitus (T2DM), dyslipidaemia, and metabolic dysfunction-associated steatotic liver disease (MASLD) are increasingly recognised as chronic inflammatory conditions driven in part by innate immune dysregulation. Among the metabolic factors implicated in this process, branched-chain amino acids (BCAAs) have emerged as key regulators linking nutrient sensing to immune cell function. Circulating BCAA concentrations are consistently elevated in these metabolic diseases. However, experimental and clinical studies also show that BCAA supplementation can improve metabolic and immune outcomes in specific contexts, revealing a paradoxical relationship between BCAA metabolism and inflammation. This narrative review examines how dysregulated BCAA metabolism and accumulation of branched-chain keto acids (BCKAs) shape the functional programming of innate immune cells across these conditions, including monocytes/macrophages, granulocytes, dendritic cells, and natural killer cells. Evidence indicates that the immunometabolic effects of BCAAs depend not solely on circulating concentrations but on the efficiency of their intracellular catabolism. When BCAA oxidation is preserved, these amino acids support mitochondrial metabolism and immune competence. Conversely, impaired catabolism leads to the accumulation of branched chain ketoacids, which activate inflammatory pathways and contribute to metabolic dysfunction. Resolving this paradox requires the need of targeting catabolic flux restoration rather than simple BCAA restriction or supplementation, and requires stratifying patients by enzymatic capacity, BCAA/BCKA ratios, and disease stage. Pharmacological modulators, including BCKDK inhibitors and BCAT1-targeted agents, show promise in simultaneously addressing metabolic and immune dysregulation. - Source: PubMed
Publication date: 2026/04/13
Magnolia Martínez-AguilarZeinab AbdullahHans BlokzijlHan Moshage - T-cell acute lymphoblastic leukemia (T-ALL) is an aggressive, life-threatening hematological malignancy with limited therapeutic regimens. While metabolic reprogramming is known to play critical roles in leukemogenesis, how distinct metabolic pathways orchestrate T-ALL pathogenesis remains largely unknown. We herein aim to unravel how the branched-chain amino acid (BCAA) metabolism fine-tunes T-ALL cell fates. - Source: PubMed
Publication date: 2026/04/13
Dan SijiaXu YiluXie LiHe XiaoxiaoLiu HaotianZhao LuCao LiyuanQu BoLu YanChen ChiqiYu ZhuoWan JiangboChen PuZheng Junke - Bisulfite conversion remains the gold standard method for DNA methylation analysis but has known limitations. Enzymatic conversion has recently been developed and overcomes some of these pitfalls. This study compared both methods by measuring known colorectal cancer (CRC) methylated biomarkers in colorectal tissues. - Source: PubMed
Publication date: 2026/03/27
Vitaro StelleneLaven-Law GeraldineKichenadasse GanessanCornthwaite KathrynSymonds Erin LWinter Jean M