Ask about this productRelated genes to: RHOA antibody
- Gene:
- RHOA NIH gene
- Name:
- ras homolog family member A
- Previous symbol:
- ARH12, ARHA
- Synonyms:
- RhoA, Rho12, RHOH12
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1990-03-19
- Date modifiied:
- 2019-04-23
Related products to: RHOA antibody
Related articles to: RHOA antibody
- To evaluate whether hybrid models integrating deep learning (DL) features from baseline radiographs and demographic information can predict incident radiographic hip osteoarthritis (RHOA) and to compare their performance to models using radiographic or demographic information in isolation. - Source: PubMed
Publication date: 2026/09/16
van den Berg Myrthe Avan Tulder GijsAhedi HarbeerArden Nigel KBierma-Zeinstra Sita M ABoel FleurBoer Cindy Gvan Buuren Michiel M ACicuttini Flavia MCootes Timothy FFelson David TGielis Willem PaulHeerey JoshuaKemp JoanneJones GraemeKluzek StefanLane Nancy ELindner Claudiavan Meurs Joyce B JMosler Andrea BNelson Amanda ENevitt Michael COei Edwin HRunhaar JosWeinans HarrieKrijthe Jesse HAgricola Rintje - Solid tumors are highly dynamic environments, in which endothelial cells (ECs) interface with blood, cancer cells, and the extracellular matrix (ECM), thereby regulating tumor behavior and metastatic dissemination. We recently showed that aberrant Vascular Endothelial Growth Factor Receptor 2 (VEGFR2) activation promotes tumor progression through ECM remodeling. Here we investigated whether VEGFR2-driven ECM remodeling affects EC behavior and vessel stability. Using decellularized ECM from Sk-Mel-31 melanoma cells expressing either VEGFR2 or the aberrant VEGFR2 mutant, we found that VEGFR2 reshapes ECM composition, including core matrisome components, ECM-modifying enzymes, and vascular-associated proteins. ECs seeded on VEGFR2-derived ECM displayed altered adhesion dynamics, characterized by focal adhesion remodeling, increased haptotaxis, and impaired morphogenic capacity. This remodeled ECM also induced cytoskeletal reorganization, disruption of VE-cadherin junctions via RhoA activation. Consistently, VEGFR2-derived tumors exhibited more immature vessels with discontinuous junctions and the expression of mesenchymal markers. Under laminar flow, ECs exposed to VEGFR2-ECM showed a delayed calcium dynamic and Yap localization, defective polarization, actin alignment, and impaired shear-stress adaptation. Overall, these findings identify VEGFR2-driven ECM remodeling as a non-cell-autonomous mechanism that destabilizes tumor vasculature by impairing endothelial adhesion, mechanosensing, and junctional integrity, highlighting tumor/ECM/endothelium crosstalk as a potential therapeutic vulnerability. - Source: PubMed
Publication date: 2026/09/24
Domenichini MattiaCorsini MichelaRavelli CosettaRicci AnastasiaMoreschi ElisaGrillo ElisabettaMaggi CamillaBaldanzi GianlucaChiodini SoniaSanchez-Amador Diana EvelineKraxner JuliaMonaghan Michael GGerhardt HolgerMenotta MicheleMitola Stefania - Sphingosine-1-phosphate lyase insufficiency syndrome (SPLIS) is a rare condition causing nephrotic syndrome, neuropathy, and other manifestations. SPLIS is caused by mutations in SGPL1, which encodes sphingosine-1-phosphate lyase (SPL), a pyridoxal 5'-phosphate (PLP)-dependent enzyme needed to degrade the bioactive sphingolipid sphingosine-1-phosphate (S1P). Supplementation with the PLP precursor pyridoxine benefits some individuals with PLP-dependent enzymopathies. We investigated whether pyridoxine has therapeutic activity in SPLIS. Neurological improvement, plasma S1P normalization, and increased SPL activity in patient-derived fibroblasts were observed after pyridoxine supplementation in a patient with R222Q-variant SPLIS. Additionally, PLP dose-dependently augmented recombinant R222Q-variant SPL activity. To further explore pyridoxine's effects, gene editing was employed to create an R222Q-variant SPLIS mouse model. SPLR222Q mice fed pyridoxine-enriched chow lacked obvious phenotypes. However, SPL inactivation, S1P accumulation, proteinuria, and glomerulosclerosis developed in SPLR222Q but not WT mice fed chow with reduced pyridoxine. Ultrastructural analysis and super-resolution microscopy showed podocyte loss and foot process effacement. Transcriptional profiling revealed patterns of cytokine upregulation and extracellular matrix remodeling. Inhibiting S1P production or RhoA/ROCK signaling prevented nephrosis in SPLR222Q mice fed chow lacking pyridoxine. Our findings establish a SPLIS mouse model that recapitulates R222Q-variant SPLIS, demonstrates its responsiveness to pyridoxine, and implicates a S1P/RhoA/ROCK pathway in its pathophysiology. Running Title: Cofactor supplementation in R222Q-variant SPLIS. - Source: PubMed
Publication date: 2026/09/24
Khan RanjhaAllende Maria LKhalid EhteshamLee Joanna YStone EverettRodnick-Smith MaxIzuhara AudreyBuncha VadymGyarmati GeorginaPeti-Peterdi JanosAl-Khaledy RanyaHodgin Jeffrey BTassew GizachewOskouian BabakChen AlinaChang Yu-TangZhang RachelProia Richard LSaba Julie D - Titanium dioxide nanoparticles (TiO NPs) are ubiquitous dietary additives, yet their impact on the intestinal barrier remains contentious, largely because conventional toxicological models overlook gastrointestinal digestive transformations. Characterization revealed that pristine TiO NPs exist as nanoscale aggregates, which, upon simulated digestion, lose electrostatic repulsion and expand into dense, biocorona-coated, micrometer-sized agglomerates enriched in nitrogen and phosphorus. While these transformed entities induce severe barrier dysfunction, the spatiotemporal mechanisms executing plasma membrane rupture remain a critical knowledge gap in nanotoxicology. Here, we uncover a non-canonical, spatially dependent cell death modality termed mitoxyperilysis as the core driver of TiO NPs-induced nanotoxicity, operating independently of classical apoptosis, ferroptosis, necroptosis, and pyroptosis. We demonstrate that exposure to digested TiO NPs agglomerates hyperactivates the protein kinase B (AKT)/mechanistic target of rapamycin complex 2 (mTORC2)-RhoA signaling axis, leading to widespread F-actin cytoskeletal paralysis. This structural breakdown dismantles intracellular spatial constraints, enabling ROS-emitting, dysfunctional mitochondria to aberrantly translocate and persistently tether to the plasma membrane, deploying high concentrations of mitochondria-derived ROS (mtROS) locally. Quantitative lipidomics of plasma membrane fractions reveals that this targeted mtROS assault induces severe depletion of membrane-stabilizing lipids and the explosive generation of oxidized lipid mediators, culminating in lytic membrane failure. Ultimately, this nanotoxicology study decodes a novel nano-mechanopathological paradigm dictated by mTOR-cytoskeleton dysregulation and localized mitochondrial lipid peroxidation, providing critical translational insights and therapeutic targets for mitigation. - Source: PubMed
Publication date: 2026/09/15
Zhang ChuxinLiu YipingLi XuAn JiaxingLi WenjingZhou ZhiluYan YitaoShao JuanGuo Zhongyuan - Bladder cancer (BC) is one of the most deadly diseases in the USA, with 84,530 new cases and 17,870 estimated deaths in 2026. The growth factor progranulin is involved in several human pathologies, including frontotemporal dementia (FTD), immune response, and cancer. We showed that in BC, progranulin and its signaling receptor, EphA2, drive tumor cell motility, invasion, and in vivo tumor formation, making it a critical pathway in tumor establishment. However, the molecular mechanisms of progranulin/EphA2 action are still poorly defined. - Source: PubMed
Publication date: 2026/08/11
Satasiya VrundaMartinelli CanioPascal GabrielDucci GiacomoVentura ElisaWilliams Stephen JBurk Sharon RaffaellaTchamou Manuela NanaShani ShendiKlain MicheleSacco ElenaVanoni MarcoBelfiore AntoninoIozzo Renato VGiordano AntonioMorrione Andrea