HDLBP antibody
- Known as:
- HDLBP (anti-)
- Catalog number:
- orb101741
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- HDLBP antibody
Related genes to: HDLBP antibody
- Gene:
- HDLBP NIH gene
- Name:
- high density lipoprotein binding protein
- Previous symbol:
- VGL
- Synonyms:
- HBP
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-12-01
- Date modifiied:
- 2015-09-11
Related products to: HDLBP antibody
Related articles to: HDLBP antibody
- Ferritinophagy is crucial for maintaining iron homeostasis and regulating iron-dependent viral replication. This study demonstrates that ferritinophagy reprograms carnitine-dependent lipid metabolism by impairing Fe-S clusters biogenesis, thereby inhibiting iron-dependent viral replication. Specifically, NCOA4-mediated ferritinophagy disrupts Fe-S clusters assembly through the autophagic degradation of MMS19, leading to mitochondrial metabolic remodeling and suppression of carnitine biosynthesis. Carnitine deficiency subsequently destabilizes the proteins TMED10, HDLBP, and RAB40C via specific amino acid residues (Asp78, Leu336, and Glu154, respectively), and we reveal that carnitine directly stabilizes these lipid droplet-associated proteins, promoting lipid droplet formation. Collectively, these changes orchestrate an iron-lipid metabolic axis that inhibits the replication of diverse PRRSV strains as well as influenza A virus (IAV). Conversely, PRRSV counteracts this antiviral mechanism by promoting autophagic degradation of NCOA4 via K63-linked ubiquitination, a process in which the viral protein Nsp5 recruits the E3 ligase adaptor DDB1 to mediate ubiquitination. Our findings establish NCOA4 as a link between ferritinophagy and lipid metabolic reprogramming, revealing a novel antiviral pathway and providing foundational insights for developing innovative antiviral strategies. - Source: PubMed
Publication date: 2026/05/20
Guan KaifengYuan ChenyangMeng ZekunWang YananZhai XueyingHuang ChunjieZhou XiangZhang Gaiping - Long duration spaceflight leads to significant muscle mass and strength loss, which current inflight countermeasures can only partially mitigate. This study aimed to identify as yet unexplored low-abundance serological biomarkers in astronaut blood samples as meaningful biological signatures for deeper insight into musculoskeletal adaptation as complementary protocol for upgraded health monitoring in future spaceflight. - Source: PubMed
Publication date: 2026/04/22
Moriggi ManuelaCapitanio DanieleTorretta EnricaMetatla InesFrings-Meuthen PetraHeinz ViktorTrautmann GaborSalanova MicheleBlottner DieterGelfi Cecilia - The circadian rhythm and lipid metabolism in organisms are tightly coupled, yet the role of lncRNAs in the integration of these two important physiological processes remains unclear. In this study, we identified a liver-specific lncRNA named HlncRNA-1, which regulates lipid metabolism while responding to circadian rhythms. Mice overexpressing HlncRNA-1 exhibited suppressed liver fat accumulation under conditions of both nutrient surplus and deficiency, along with improved insulin sensitivity. At the molecular level, ChIP assays demonstrate that Dhx9 directly occupies the HlncRNA-1 promoter, tethering circadian clock signals to this lncRNA. HlncRNA-1 subsequently recruits Hdlbp to coordinate hepatic lipid catabolism. In summary, HlncRNA-1 serves as a regulatory conduit that translates circadian clock cues into metabolic outputs, orchestrating circadian control of hepatic lipid metabolism, and activating this lncRNA represents a viable target for precisely intervening in lipid metabolic disorders induced by circadian disruption. - Source: PubMed
Publication date: 2026/05/06
Sun ChenMao ShuyuBo JiaqiangSong MingmingLiu Chang - High-density lipoprotein-binding protein (HDLBP), also called Vigilin, is a multifunctional RNA-binding protein with established roles in RNA transport and regulation, chromosome segregation, lipid homeostasis, and translational regulation. Frequently detected to be perturbed in phosphoproteome analysis, phosphorylation is indicated as a major mechanism in the regulation of HDLBP functions; however, its phosphorylation landscape remains unexplored. We performed a meta-phosphoproteome analysis of HDLBP to map site-specific functional and regulatory roles of its two most frequently detected phosphosites, S31 and S944. Co-occurrence analysis across multiple datasets indicated that they can be phosphorylated together, suggesting potential co-ordinated regulation. Site-specific co-regulation analysis revealed distinct phospho-regulatory networks, with upstream kinases identified exclusively for S944. Functional enrichment of co-regulated protein phosphosites (CPPs) highlighted its role in RNA metabolism, chromosome organization, and nucleoplasmic transport, while functional annotation of site-specific phosphorylation of CPPs indicates its involvement in cell cycle regulation, apoptosis, and carcinogenesis. Additionally, the potential role of CPPs in the lipid homeostasis network was explored. Furthermore, the differential expression of HDLBP phosphosites across multiple cancers was observed using UALCAN, suggesting a potential role for phospho-regulation of HDLBP in tumor-associated pathways. Together, these findings provide the first integrated view of HDLBP phosphorylation and could serve as a valuable framework for future targeted studies to elucidate the mechanistic roles of site-specific HDLBP phosphorylation in cellular and pathophysiological processes. - Source: PubMed
Publication date: 2026/02/25
Sekhar Pathiyil SajiniFahma AmalSubair SuhailDcunha LeonaMahin AlthafGopalakrishnan Athira PerunallyRaju RajeshSoman Sowmya - In pancreatic ductal adenocarcinoma, hypoxia is a crucial component of the tumour microenvironment and is associated with worse clinical outcomes. Adaptation to extreme hypoxic settings is based on abnormal lipid metabolism, but insights into how hypoxia-regulated lipid changes link with aggressive migratory potential in pancreatic cancer are lacking. This study investigates the molecular processes, pathways, and critical proteins involved in hypoxia-induced lipidic and polyunsaturated fatty acid alterations in pancreatic cancer. Our findings elucidate increased multilayer unsaturation in FA chains of major lipid classes associated with greater migration and invasion, as well as higher abundances of particular desaturases. The expression of these proteins was verified in clinical tumour samples by unsaturated fatty acid biosynthesis-related gene enrichment score. High unsaturated fatty acid clusters were shown to be associated with a low survival rate. Pathway correlation and protein-protein interaction analysis indicated that the PPAR-hypoxia axis and SCD/FADS2/APOC3-HDLBP protein network are implicated in mediating the observed alterations in lipid pools and poly-unsaturation levels in pancreatic cancer under hypoxia. These results provide novel therapeutic targets in pancreatic cancer while improving our understanding of hypoxia-induced migratory potential in pancreatic cancer. - Source: PubMed
Publication date: 2025/12/01
Agarwala Prema KumariSingh AvinashSrivastava SanjeevaKapoor Shobhna