Ask about this productRelated genes to: LPCAT1 antibody
- Gene:
- LPCAT1 NIH gene
- Name:
- lysophosphatidylcholine acyltransferase 1
- Previous symbol:
- AYTL2
- Synonyms:
- FLJ12443, AGPAT9, AGPAT10
- Chromosome:
- 5p15.33
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-03
- Date modifiied:
- 2015-08-26
Related products to: LPCAT1 antibody
Related articles to: LPCAT1 antibody
- - Source: PubMed
Publication date: 2026/04/15
Jiang LipingXu SumeiPeng JingboYu JingWu HuilanWu WeiHuang ZhichunPan JieTan Zhirong - Mitochondrial dysfunction plays a critical role in hepatocellular carcinoma (HCC) progression. This study aimed to identify mitochondrial-related prognostic genes and elucidate their functional mechanisms in HCC. Mitochondrial-related prognostic genes were screened from the TCGA and ICGC-LIHC cohorts. A prognostic risk model was constructed and validated in three external cohorts. Immunotherapy sensitivity between high- and low-risk groups was assessed using somatic mutation and immune infiltration analyses. Underlying molecular mechanisms were further validated through in vitro experiments in HCC cell lines. Transcriptome analysis identified 15 mitochondrial-related prognostic genes, from which 10 candidates were refined using LASSO regression. Among them, LPCAT1 and MRPL9 were significantly associated with overall survival. The 2-MRG model (comprising LPCAT1 and MRPL9) demonstrated superior prognostic accuracy and better survival stratification across both internal and external cohorts. Functional enrichment analysis revealed significant metabolic dysfunction in the high-risk group. The high-risk group also exhibited a significantly higher tumor mutation burden and an enhanced predicted responsiveness to immunotherapy. In vitro, knockdown of MRPL9 or LPCAT1 inhibited the proliferation and migration of HCC cells by inducing G1/S arrest and G2/M arrest, respectively. Moreover, they also suppressed the AKT phosphorylation. We developed a robust 2-MRG prognostic model based on LPCAT1 and MRPL9 that effectively predicts HCC outcomes and supports individualized therapeutic decision-making. Both genes promote HCC progression by modulating the AKT phosphorylation and cell-cycle checkpoints, highlighting their potential as therapeutic targets. - Source: PubMed
Publication date: 2026/04/02
Yang HuiZhu ZiqiZhu HanwenLi NanjingZheng SinianHu LingWu ZhenruShi Yujun - ATP-citrate lyase (ACLY) is a crucial cytosolic and nuclear enzyme that catalyzes the synthesis of acetyl-CoA from citrate, serving as a central metabolic node linking carbohydrate metabolism to lipogenesis and histone acetylation. Accumulating evidence positions ACLY not merely as a metabolic enzyme but as a key pathogenic driver in various kidney diseases. This review systematically examines the multifaceted roles of ACLY in renal physiology and pathology. During development, ACLY is essential for nephron progenitor cell maintenance and nephrogenesis. In diabetic kidney disease, hyperglycemia upregulates and promotes nuclear translocation of ACLY, fueling histone acetylation and the transcription of pro-fibrotic genes, while also contributing to oxidative stress and lipid peroxidation. In obesity-related kidney injury, ACLY drives renal ectopic lipid accumulation and inflammation by providing substrates for adipogenic enzymes and inducing histone hyperacetylation. ACLY also promotes renal fibrosis in chronic kidney disease pathways such as AKT/ACLY signaling. In clear cell renal cell carcinoma, ACLY expression is upregulated through HIF-2α/LPCAT1/FBXW7 and VHL/PPARγ axes, promoting lipid synthesis, tumor proliferation, and metastasis. Furthermore, ACLY activity influences hypocitraturia, a key factor in nephrolithiasis, and is upregulated in polycystic kidney disease, where its inhibition attenuates cystic growth. Given its central role across diverse renal pathologies, ACLY emerges as a promising therapeutic target. Several inhibitors, including bempedoic acid, SB-204990, and natural compounds, show potential in modulating ACLY activity. This review consolidates current knowledge on ACLY in kidney diseases, highlighting its mechanistic contributions, and underscoring its significant potential for diagnostic and therapeutic innovation. - Source: PubMed
Publication date: 2026/04/09
Wei MengjiaoTao MinaTan HuifangJin ZhiyuanYang YiyaXiao ZhengLi GuoliChen Yinyin - - Source: PubMed
Publication date: 2026/04/02
Wang XiaowenXue MingshanSu LijunLuo XianLi YouxiaFan ShaohuiHu QiurongLiao HuizhaoJiang ChuciChen JiahongSun BaoqingLi ShaoqiangWang Hongman - Absence of the endosomal SNAREs vti1a and vti1b results in perinatal death and severe neuronal phenotypes in mice, while lack of one of these proteins results in minor phenotypes. Proteomic differences were investigated to obtain a deeper insight into processes in which vti1a and vti1b are involved. Here we applied a bottom-up shotgun proteomic approach to investigate the differences in wild-type, double heterozygous (DHET), vti1a vti1b double knockout (DKO), vti1a knockout and vti1b knockout cerebral cortices. Single deletions did not affect protein levels significantly. A total of 1725 proteins were detected of which 69 were less abundant and 191 proteins were more abundant in DKO cortices. Many less abundant proteins belonged to cellular components and reactome pathways synapse, synaptic vesicle cycle, vesicle mediated transport, L1CAM interaction, and cholesterol biosynthesis in pathway enrichment analysis. More abundant proteins were enriched in cellular components and Kyoto Encyclopaedia of Genes and Genomes (KEGG)-pathways such as spliceosome, ribosome, carbon metabolism, and ribonucleoprotein complex. Immunoblotting validated reduced expression levels of the tested synaptic vesicle proteins as well as increased amounts of lysophosphatidylcholine acyltransferase 1 (Lpcat1) and neuron-specific gene 2 (Nsg2), which is involved in postsynaptic AMPA-receptor recycling. These data indicate that the synapse and cell adhesion were strongly affected in DKO brains. STATEMENT OF SIGNIFICANCE OF THE STUDY: Distinct populations of neurons and glia cells are generated and organize into layers during brain development. Neurons develop an elaborate morphology to transmit information via axons and synapses to dendrites in receiving neurons. These neurites form via several specialized pathways of vesicle secretion and endocytosis. Fusion between these membranes requires members of the SNARE protein family. Double knockouts of the endosomal SNAREs vti1a and vti1b (DKO) result in perinatal lethality in mice with massive defects in the brain. In this study we compared the proteome of DKO brain cortices with double heterozygous controls to obtain insights into the molecular alterations and affected pathways. DKO brains contained lower amounts of synaptic proteins and proteins involved in cell adhesion, membrane trafficking and cholesterol biosynthesis. Several proteins of spliceosomes, ribosomes and carbon metabolism were more abundant in DKO brains, which may be a consequence of the reduced amounts of synaptic proteins or a shift in cell populations. Lysophosphatidylcholine acyltransferase 1 (Lpcat1) and neuron-specific gene 2 (Nsg2), which is involved in α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) recycling, were confirmed to be more abundant by Western blotting. These data point to defects in trafficking especially in the synapse and in cell adhesion, which is required for neurite outgrowth. - Source: PubMed
Publication date: 2026/03/20
Gottschalk JuliaKotschnew KatharinaHahn JuliaPatschkowski Thomasvon Fischer von Mollard Gabriele