Ask about this productRelated genes to: LPCAT4 antibody
- Gene:
- LPCAT4 NIH gene
- Name:
- lysophosphatidylcholine acyltransferase 4
- Previous symbol:
- AYTL3, AGPAT7
- Synonyms:
- FLJ10257, LPAAT-eta, LPEAT2
- Chromosome:
- 15q14
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-03
- Date modifiied:
- 2014-11-19
Related products to: LPCAT4 antibody
Related articles to: LPCAT4 antibody
- Microplastics (MPs) derived from film mulching commonly exist in cadmium (Cd)-contaminated agricultural soil, but their impacts on Cd phytotoxicity are still controversial. Lipid remodeling is a key plant stress response, but whether conventional and biodegradable MPs differently regulate this process under Cd stress remain unclear. This study compared the effects of conventional polyethylene (PE) and biodegradable polylactic acid (PLA) MPs at two concentrations (0.1% and 1%) on Cd phytotoxicity in maize via a 35-day pot experiment, mainly focusing on the lipid homeostasis. Both individual and combined exposures to MPs and Cd inhibited maize growth and photosynthesis and induced oxidative stress. PE significantly reduced Cd concentration (20.06-38.71%) and uptake content (27.22-39.77%) in shoots and roots. PLA exhibited dose-dependent effects, where 0.1% addition increased Cd accumulation in roots, while 1% addition decreased it in shoots. These effects might be attributed to altered homeostasis of essential minerals (Ca, Fe, and Cu). Interaction analysis revealed that PE acted antagonistically with Cd at 0.1% and synergistically at 1%, while PLA showed antagonism at both concentrations. Integrated lipidomic and transcriptomic analyses identified five key regulatory genes (LACS4, GPAT6, LPP2, PLA2-III, and LPCAT4) significantly associated with 36 glycerophospholipids and glycerolipids, revealing that PE and PLA influenced maize molecular response via distinct lipid metabolism pathways under Cd stress. These findings demonstrate that conventional and biodegradable MPs differentially regulate Cd phytotoxicity in Cd‑contaminated soils through lipid remodeling, providing new insights for the safety assessment of agricultural film mulching. - Source: PubMed
Publication date: 2026/05/21
Li HuijunZheng XiaodieShan HonghongHuang YichaoMa ChuanxinZhao JianHuang Xiaochen - Major membrane phospholipids (PLs) contain saturated FAs, such as palmitic acid (C16:0) and stearic acid (C18:0), at the sn-1 position. Although atypical PLs containing unsaturated FAs at the sn-1 position exist as minor components, the biosynthetic pathway responsible for their production has remained elusive. Here, we report that LPLAT10 (also known as LPEAT2 or LPCAT4) is a lysophospholipid acyltransferase responsible for generating PLs with an unsaturated FA at the sn-1 position. In vitro, LPLAT10 incorporated both saturated and unsaturated FAs into lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine, selectively at the sn-1 position. LPLAT10 appeared to have a relatively higher affinity for unsaturated FA-CoAs. Consistently, only PLs with unsaturated FAs such as oleic acid (C18:1), linoleic acid (C18:2), arachidonic acid (C20:4), and DHA (C22:6) at the sn-1 position decreased in the brain from Lplat10-deficient mice. Despite their low abundance, these atypical PLs may have specific roles, given that LPLAT10 is highly expressed in neurons and its encoding genes are highly conserved among vertebrates above fish. - Source: PubMed
Publication date: 2026/02/23
Kawana HirokiKataoka RikutaSato YukitakaOnishi HirofumiIwama TaigaShimanaka YutaSaigusa DaisukeKano KuniyukiKono NozomuAoki Junken - The uterus is a pivotal organ for mammalian reproduction, directly determining reproductive success by orchestrating embryo implantation, placental development, fetal nourishment, and parturition. However, the molecular mechanisms regulating high fecundity in the uterus across different stages of the estrous cycle remain unclear. This study aimed to elucidate the genetic regulation of goat fecundity through integrated proteomic and transcriptomic analyses of uterine tissues. - Source: PubMed
Publication date: 2026/02/21
Zou DongbinDu XiaolongLiu YufangFang MeiyingChu Mingxing - X-linked adrenoleukodystrophy (X-ALD) is a congenital metabolic disorder characterized mainly by inflammatory demyelination and adrenal insufficiency. Newborn screening using hexacosanoyl lysophosphatidylcholine (C26:0-LPC) in dried blood spots as a diagnostic marker can successfully identify potential patients with X-ALD and prevent disease onset. C26:0-LPC accumulates in patients with X-ALD, although the machinery synthesizing it has remained unclear. In this study, we focused on phosphatidylcholine (PC) with C26:0 moiety as a precursor of C26:0-LPC. We identified that lysophospholipid (LPL) acyltransferase 10 (LPLAT10)/LPCAT4/LPEAT2/AGPAT7 (1-acylglycerol-3-phosphate O-acyltransferase 7) is the responsible LPL acyltransferase that produces PC with C26:0 moiety by transferring C26:0-CoA into 2-acyl-LPC. We also found that LPLAT10 deficiency decreased the amount of C26:0-LPC in fibroblasts from X-ALD patients. Mechanistically, LPLAT10 introduced saturated fatty acid-CoA of various chain lengths as substrates into the sn-1 position of LPC but did not transfer C26:0-CoA to other LPL classes, such as lysophosphatidylethanolamine. Structural analysis revealed that a trimethylamine group of PC was placed between two tryptophan residues (W242 and W244), forming a W-X-W motif, possibly through cation-π interaction. Finally, it was shown that exogenously administered C26:0 FFA-d was preferentially incorporated into sphingolipids in the absence of LPLAT10. These results suggest that C26:0-LPC is produced through acyl-chain remodeling of PC catalyzed by LPLAT10 and accumulates in the plasma from X-ALD patients. - Source: PubMed
Publication date: 2025/12/30
Hama KotaroFujiwara YukoImai KokoKusakabe YoshioHayashi YasuhiroTakashima ShigeoAzuma ShoheiKondo MasaruYamashita AtsushiTakita RyoShimozawa NobuyukiYokoyama Kazuaki - The structure and function of cellular and intracellular membranes are critically governed by the fatty acid (FA) composition of phospholipids (PLs), which is dynamically regulated by a network of enzymes that fine-tune lipid species according to cellular demands. In this study, we identify a mechanism through which the formation of mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) modulates the activity of the acyl-CoA synthetase long-chain family member 4 (ACSL4), an enzyme that channels polyunsaturated fatty acids (PUFAs) into phosphatidylcholine (PC) via the Lands cycle. Through integrated biochemical, proteomic, and lipidomic analyses in both cellular and animal models, we demonstrate that MAM formation enhances ACSL4 activity, promoting arachidonic acid (AA) activation and its preferential incorporation into PC in concert with the MAM-localized lysophospholipid acyltransferase 4 (LPCAT4). Our findings further uncover an unexpected link between this pathway and the pathogenesis of Alzheimer's disease (AD). We show that elevated levels of C99-the β-secretase cleavage product of amyloid precursor protein (APP)-induce MAM remodeling through cholesterol clustering, which in turn activates ACSL4 and alters PC composition. This effect is mirrored in AD models as well as in fibroblasts, neurons, and immune cells derived from both familial and sporadic AD patients, all of which exhibit chronically increased C99 levels, heightened ACSL4 activity, and enrichment of PUFA-containing PC species, leading to lipid imbalance and membrane dysfunction. Together, these results establish MAMs as dynamic lipid-regulatory hubs that coordinate ACSL4-dependent membrane remodeling and highlight the contribution of MAM dysregulation to lipid abnormalities observed in AD. - Source: PubMed
Publication date: 2025/11/27
Montesinos JYun T DSalomón-Cruz I DAgudelo-Castrillón S CUceda MFerre A CAnton-Barros CGomez-Lopez NAgrawal R RLarrea DVelasco K RFernàndez-Bernal ABenitez EZhu XSchon E ALopera FCardona-Gomez G PArea-Gomez E