Ask about this productRelated genes to: Pcyt2 antibody
- Gene:
- PCYT2 NIH gene
- Name:
- phosphate cytidylyltransferase 2, ethanolamine
- Previous symbol:
- -
- Synonyms:
- ET
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-06-09
- Date modifiied:
- 2016-04-01
Related products to: Pcyt2 antibody
Related articles to: Pcyt2 antibody
- Non-alcoholic fatty liver disease (NAFLD) represents a burgeoning global health burden with limited pharmacological options. Ergothioneine (EGT), a naturally occurring antioxidant, shows potential hepatoprotective effects; however, the exact mechanisms by which EGT regulates lipid metabolism in NAFLD remain elusive. - Source: PubMed
Publication date: 2026/04/25
Ye RongyiWang YihanWang KeboHuang NanLiu GuoGao DexinLi XinruYang MengxueWang JingChen Chen - Phosphatidylethanolamine (PE) biosynthesis is critical for membrane biology and cellular homeostasis. However, its specific role in antiviral innate immunity remains poorly understood. Here, we demonstrate that inhibition of phosphoethanolamine cytidylyltransferase 2 (PCYT2), a key enzyme in PE biosynthesis, promotes TBK1 activation to enhance the antiviral innate immune response. Mechanistically, PCYT2 deficiency leads to the accumulation of diacylglycerol, which activates protein kinase C-δ (PKCδ). We identify PKCδ as a direct kinase for TBK1 and demonstrate that it binds to and phosphorylates TBK1 at Ser716. This Ser716 phosphorylation facilitates the subsequent canonical phosphorylation of TBK1 at Ser172, resulting in hyperactivation of the TBK1-IRF3 axis. Our findings uncover a link between PE metabolism and antiviral innate immunity, suggesting that targeting the PE biosynthesis pathway could be a potential therapeutic strategy against viral infections. - Source: PubMed
Publication date: 2026/05/26
Lai WencongLiu ZengjieHu HanZhang WanxuanLi BaolinWang RuiZhao ZengqiLi XueshanHu YihangDuan JinweiXu DanLiu YongtaoBu XianyongDu JianlongYang BingyuanTang XiaoLi YueruWan MinZhang YanjiaoZhou HuihuiMai KangsenAi Qinghui - Phosphoethanolamine (pETN), an endogenous metabolite in the Kennedy pathway for membrane phospholipid synthesis, can be chemically synthesized and exemplifies translational pharmacology through its journey from basic biochemistry to clinical application. Initially recognized for phosphatidylethanolamine biosynthesis via PCYT2-mediated conversion, pETN gained clinical attention following reports of Brazilian cancer patients with pETN-containing products. Subsequent pharmacological studies revealed favorable safety profiles in preclinical and clinical settings, with oral bioavailability of 6%-7%. Mechanistic investigations identified pETN as a competitive inhibitor of succinate dehydrogenase (complex II and Krebs cycle), providing molecular rationale for its mitochondrial effects. This discovery opened new therapeutic avenues beyond oncology, particularly in ischemia-reperfusion injury, where pETN's succinate dehydrogenase inhibitory activity could mitigate pathological succinate accumulation and subsequent oxidative damage during reperfusion. The translational trajectory of pETN, from endogenous metabolism through clinical observation to mechanistic understanding, exemplifies the bidirectional nature of modern pharmacological research and positions this naturally occurring compound as a promising therapeutic candidate for mitochondrial dysfunction-related conditions. - Source: PubMed
Publication date: 2026/04/23
Rossini Guilherme AyresKoike MarciaBarbeiro Denise FBarbeiro HermesRabelo DanielSoriano Francisco GarciaCesar Machado Marcel CerqueiraMaria Durvanei Augusto - High dietary sugar intake is recognized as an important risk factor for cardiovascular disease, yet the precise mechanisms that drive these pathologies remain incompletely understood. To delineate the molecular impact of hyperglycemia on the myocardium, we analyzed RNA-sequencing data from hiPSC-derived cardiomyocytes of a diabetic model (GSE288708). The analysis revealed a marked downregulation of Pcyt2 mRNA in cardiomyocytes exposed to a hyperglycemic environment. In vivo validation in Drosophila showed that a high-sugar diet (HSD) suppresses expression of Pect-the Drosophila homolog of human Pcyt2-in the heart, and that Pect knockdown reproduces HSD-induced metabolic disturbances and cardiac dysfunction. An exercise regimen partially rescued the cardiac phenotype: exercise restored cardiac Pect expression and phosphatidylethanolamine (PE) content, preserved mitochondrial integrity and redox homeostasis, and ameliorated cardiac fibrosis and functional decline. Notably, cardiac-specific knockdown of Pect impeded the ability of exercise to confer these partial improvements, implicating the Pect/PE biosynthetic pathway as a potential therapeutic target for HSD-induced cardiomyopathy. These findings establish a previously underappreciated pathway through which diet and exercise jointly regulate heart health via Pect-PE modulation. - Source: PubMed
Publication date: 2026/03/19
Zhang ZikeDing NiDing MengPeng TianhangPing XuGu WenzhiYu ZhengwenZhang ZhilongYi QinPan ZhihaoZheng Lan - Recent studies have indicated that phosphoethanolamine cytidylyltransferase 2 (PCYT2) is aberrantly expressed in various tumors, influencing tumor progression, metastasis, and drug resistance. However, the role of PCYT2 in clear cell renal cell carcinoma (ccRCC) remains unexplored. The objective of this research is to explore the expression changes of PCYT2 in ccRCC and elucidate its potential regulatory effects on ccRCC biological functions, alongside the underlying molecular mechanisms. Through sequencing data analysis and clinical tissue assessments, we discovered a notable downregulation of PCYT2 in ccRCC tissues, with lower PCYT2 expression correlating with poorer patient prognosis. Gene overexpression and silencing experiments demonstrated that PCYT2 overexpression exerted notable anti-cancer effects, including inhibition of cell proliferation, migration, and invasion. Silencing PCYT2 produced opposite effects, which could be reversed by PCYT2 overexpression. Mechanistic studies revealed that PCYT2 promoted the phosphorylation of Yes-associated protein 1 (YAP1), preventing its nuclear translocation and thereby inhibiting YAP1 pathway activation. Further investigations indicated that the regulatory effect of PCYT2 on YAP1 phosphorylation was dependent on PPP2R1A. In vivo studies corroborated these findings, showing that PCYT2 overexpression significantly restrained tumor formation, accompanied by downregulation of the YAP1 pathway. Our findings offer substantial evidence that PCYT2 acts as a tumor suppressor in ccRCC, with its mechanism linked to the regulation of YAP1 pathway activation. This study offers fresh perspectives on the molecular pathogenesis of ccRCC and identifies PCYT2 as a potential candidate for therapeutic strategies in this disease. - Source: PubMed
Publication date: 2026/03/07
Nan NingGuo HaoHuang YanChen JuanQiang Xiaolong