Ask about this productRelated genes to: OSBPL8 antibody
- Gene:
- OSBPL8 NIH gene
- Name:
- oxysterol binding protein like 8
- Previous symbol:
- -
- Synonyms:
- OSBP10, ORP8, MST120, MSTP120
- Chromosome:
- 12q14
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-28
- Date modifiied:
- 2015-11-16
Related products to: OSBPL8 antibody
Related articles to: OSBPL8 antibody
- The kappa class of glutathione S-transferases 1 (GSTK1) is a vital regulatory factor in metabolic diseases. This study was conducted to investigate the regulatory effects of GSTK1 on renal ectopic fat deposition (EFD) and lipotoxic injury in diabetic nephropathy (DN) . - Source: PubMed
Publication date: 2026/04/30
Chen HongLiu YanZhao Ming-GeWu Xue-QinDai Ai-MingWang YuYang Ye-YiLi Ai-MeiZhang WeiWang Jun-PuZhou Zhi-JiaoTi-Chen Zhang HaoYang Shikun - Ferroptosis is a tumor-suppressive mechanism with therapeutic potential. While canonical ferroptosis is usually triggered by inducers, such as erastin and RSL-3, or by glutathione peroxidase (GPX)4 loss, how ferroptosis occurs naturally in vivo without these triggers has been unclear. Building on evidence that p53 can mediate ferroptosis as a natural tumor-suppressive pathway, we describe a noncanonical, in vivo ferroptosis driven by reactive oxygen species (ROS)-induced phosphatidic acid (PA) peroxidation that proceeds without inducers. We identify GPX1 as a key regulator of this ROS-induced ferroptosis by modulating PA peroxidation. GPX1's effects depend on OSBPL8, an endoplasmic reticulum (ER)-membrane-associated oxysterol-binding protein. ROS-driven lipid peroxidation accumulates at the ER before plasma membrane rupture and cell death; GPX1 is recruited to the ER via OSBPL8 and directly reduces oxidized PA. OSBPL8 and GPX1 are overexpressed in cancers; knockdown of either promotes ROS-induced ferroptosis and suppresses tumor growth. Our data link the GPX1-OSBPL8 axis to in vivo ferroptosis and tumor suppression. - Source: PubMed
Publication date: 2026/02/19
Xia ZhangchuanYang XinSamovich Sviatlana NTyurina Yulia YTyurin Vladimir AKon NingZhang JiankangJiang XuejunStockwell Brent RJin JianBayir HülyaKagan Valerian EGu Wei - Lipophagy, the selective autophagic degradation of lipid droplets (LDs), is a key mechanism for lipid homeostasis and cellular adaptation to metabolic and stress conditions. In mammals, lipophagy is governed by signaling pathways, LD-associated receptors (e.g. SQSTM1/p62, NBR1, OPTN, SPART, OSBPL8, DDHD2, VPS4A, ATG14, and TP53INP2), and transcription factors (TFEB, TFE3, FOXO1, PPARA, PPARG, and SREBF1/SREBP1) that coordinate LD recognition, sequestration, and lysosomal degradation. Dysregulated lipophagy contributes to the pathogenesis of metabolic and age-related diseases, including metabolic dysfunction-associated steatotic liver disease/nonalcoholic fatty liver disease (MASLD/NAFLD), alcoholic liver disease, diabetes, atherosclerosis, neurodegeneration and cancer. Several recent reviews have discussed lipophagy from different angles, including its roles in metabolic disorders, central nervous system diseases, and fundamental mechanisms across species. In contrast, this review focuses specifically on mammalian lipophagy by synthesizing the latest mechanistic insights into receptor-mediated recognition, transcriptional regulation, and signaling integration. We also outline unresolved questions and conceptual gaps - such as how lipophagy is selectively activated, how it coordinates with lipolysis, and whether distinct receptor codes exist in tissue- and disease-specific contexts - that remain unanswered in the current literature.: AMPK, AMP-activated protein kinase; ATG, autophagy related; ATG8s: mammalian Atg8-family proteins; C1P: ceramide-1-phosphate; CMA, chaperone-mediated autophagy; COPI, coatomer protein complex I; DENV, dengue virus; ER, endoplasmic reticulum; ESCRT: endosomal sorting complex required for transport; FFA: free fatty acid; HOPS, homotypic fusion and vacuole protein sorting; LDs, lipid droplets; LIR: LC3-interacting region; MASLD, metabolic dysfunction-associated steatotic liver disease; MTORC1: mechanistic target of rapamycin kinase complex 1; PE: phosphatidylethanolamine; PEDV: porcine epidemic diarrhea virus; PENV, porcine epidemic diarrhea virus; PtdIns3K-C1: class III phosphatidylinositol 3-kinase complex 1; PtdIns3P, phosphatidylinositol-3-phosphate; ROS, reactive oxygen species; SNARE: soluble NSF attachment protein receptor; SPG54: spastic paraplegia type 54; TAG: triacylglycerol/triglyceride; UBDs, ubiquitin-binding domains. - Source: PubMed
Publication date: 2026/02/18
Zhao RuiDai EnyongKang RuiLiu JiaoKlionsky Daniel JTang DaolinQu YangchunLin YuanqiangZhang Xinyue - Dysfunction of the neuronal macroautophagy/autophagy-lysosome system is a critical contributor to neuronal death following spinal cord injury (SCI), but the underlying mechanisms remain elusive. Our study demonstrated that SCI induced impaired autophagic flux and lysosomal membrane permeabilization (LMP) in neurons. By combining bulk RNA sequencing with validation experiments, we observed the transient upregulation of the membrane repair factor PI4K2A, which was specifically enriched in lysosomes, after SCI. Crucially, ER-MS and IP-MS analyses revealed an interaction between PI4K2A and the endoplasmic reticulum lipid transfer protein OSBPL6/ORP6. This interaction led to the transport of phosphatidylserine (PS) to damaged lysosomal membranes, promoting LMP repair and subsequently reducing lipid droplet accumulation, which suppressed neuronal death. Furthermore, overexpression of neuronal PI4K2A , through an OSBPL6- and PS-dependent mechanism, reduced LMP-mediated lipid droplet accumulation and increased neuronal survival, thereby improving functional recovery after SCI. Collectively, our findings establish the PI4K2A-OSBPL6/ORP6-PS axis as a novel and essential mechanism for lysosomal membrane repair in neurons. This pathway is crucial for maintaining neuronal lipid homeostasis and represents a promising therapeutic target for reducing neuronal loss and improving functional recovery after central nervous system trauma.: AIF1/IBA1: allograft inflammatory factor 1; Baf A1: bafilomycin A; BMS: Basso Mouse Scale; CNS: central nervous system; co-IP: co-immunoprecipitation; DEGs: differentially expressed genes; DS5: DS55980254; ESCRT: endosomal sorting complex required for transport; GFP: green fluorescent protein; HSPA5/GRP78: heat shock protein family A (HSP70) member 5; HT22: hippocampal neuronal cell line; KEGG: Kyoto Encyclopedia of Genes and Genomes; LD: lipid droplet; LC-MS: liquid chromatography-mass spectrometry; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; LGALS3/GAL3: lectin, galactoside binding, soluble 3; LLOMe: L-leucyl-L-leucine methyl ester; LMP: lysosomal membrane permeabilization; LPC: lysophosphatidylcholine; LPE: lysophosphatidylethanolamine; MFGE8/lactadherin: milk fat globule EGF and factor V/VIII domain containing; MS: mass spectrometry; NAGLU: alpha-N-acetylglucosaminidase (Sanfilippo disease IIIB); NEFH/NF200: neurofilament, heavy polypeptide; OSBPL6/ORP6: oxysterol binding protein-like 6; OSBPL8/ORP8: oxysterol binding protein-like 8; PC: phosphatidylcholine; PLA2G4A/cPLA2: phospholipase A2, group IVA (cytosolic, calcium dependent); PITT: phosphoinositide-initiated membrane tethering and lipid transport; PI4K2A: phosphatidylinositol 4-kinase type 2 alpha; PLS-DA: partial least squares discriminant analysis; PS: phosphatidylserine; PtdIns: phosphatidylinositol; PTDSS1: phosphatidylserine synthase 1; PUFAs: polyunsaturated fatty acids; RBFOX3/NeuN: RNA binding protein, fox-1Â homolog (C. elegans) 3; ROS: reactive oxygen species; SCI: spinal cord injury; SQSTM1/p62: sequestosome 1; TEM: transmission electron microscopy; TGs: triglycerides. - Source: PubMed
Publication date: 2026/02/04
Zhang HaojieKang YuZhao TianlunHuang DaoqiangHu XuantaoDi JiaweiZhang YilongLu YubaoHuang MudanLi HongYao SenyuLiu BinRong Limin - Diabetic peripheral neuropathy (DPN) is a common complication of both type 1 and 2 diabetes. DPN lacks accurate early diagnostic indicators, prompting united identification of biomarkers through transcriptomics and Mendelian randomization (MR) to inform DPN prevention and treatment strategies. - Source: PubMed
Publication date: 2025/10/30
Zhu QiujinFan ShanghengMou JingruZhao ManluLi ChangluYang BenbenShangguan YihanChen XiaCai Yulan