ARAP3
- Known as:
- ARAP3
- Catalog number:
- 001829A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ARAP3
Related genes to: ARAP3
- Gene:
- ARAP3 NIH gene
- Name:
- ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3
- Previous symbol:
- CENTD3
- Synonyms:
- FLJ21065, DRAG1
- Chromosome:
- 5q31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-10
- Date modifiied:
- 2015-09-11
Related products to: ARAP3
Related articles to: ARAP3
- N6-methyladenosine (m6A)-dependent post-transcriptional regulation is increasingly recognized as a key driver of malignant progression. However, the role and regulatory mechanism of ARAP3 in glioma remain incompletely understood. ARAP3 expression was analyzed in 112 paired glioma and adjacent tissues by qRT-PCR and Western blot. Its diagnostic and clinical relevance were evaluated using ROC analysis and clinicopathological correlation. Gain- and loss-of-function assays were performed in U87 and U251 cells to assess proliferation, clonogenicity, and invasion. IGF2BP3-dependent regulation was examined through lentiviral shRNA-mediated knockdown, RNA immunoprecipitation, m6A RNA immunoprecipitation, and actinomycin D mRNA decay assays. Xenograft models were used to validate in vivo effects. ARAP3 was significantly upregulated in glioma tissues and correlated with larger tumor size and higher WHO grade, demonstrating good diagnostic performance (AUC = 0.83). High ARAP3 predicted worse survival in TCGA glioblastoma and LGG cohorts. Silencing ARAP3 suppressed glioma cell growth, colony formation, and invasion. Mechanistically, IGF2BP3 bound to ARAP3 mRNA, maintained its m6A-dependent enrichment, and enhanced transcript stability. Overexpression of ARAP3 partially rescued the inhibitory effects of IGF2BP3 knockdown in vitro and in vivo. In the xenograft model, no obvious metastatic nodules or infiltrative lesions were observed in major organs, including the lungs, liver, spleen, kidneys, and brain. ARAP3 promotes glioma progression and is sustained by IGF2BP3-mediated m6A-dependent mRNA stabilization, highlighting the IGF2BP3-ARAP3 axis as a potential biomarker and therapeutic target. - Source: PubMed
Publication date: 2026/08/22
Li JinmiaoYu HuipingZhang JinningHuang Jincong - [This retracts the article DOI: 10.2147/OTT.S115668.]. - Source: PubMed
Publication date: 2026/05/16
- This study established an optimized process for obtaining anti-aging peptides from mushroom feet (PEMFPeps). Using response surface methodology, high yields of protein (51.31 ± 3.00%) and peptides (48.71 ± 0.17% hydrolysis degree) were achieved. In a D-galactose-induced PC12 cell aging model, the simulated digests (SID-PEMFPeps) exhibited potent anti-aging effects at a concentration of 1 mg/mL. An integrated transcriptomic and metabolomic approach was employed to systematically investigate the underlying mechanisms. The results revealed that Integrated transcriptomic and metabolomic analyses showed that SID-PEMFPeps alleviated cellular senescence through multi-dimensional regulation of transcriptional and metabolic networks. This included modulating key pathways related to oxidative stress, synaptic function, and energy metabolism (e.g., glutamatergic synapse, pentose phosphate pathway, and TCA cycle), and reversing the aberrant expression of aging-associated genes (e.g., ). Our findings demonstrate that SID-PEMFPeps are promising candidates for functional foods targeting age-related dysfunction though their efficacy and safety in vivo require further validation. - Source: PubMed
Publication date: 2025/11/20
Wang ShangmengLi HaiyanZhao FenGao Ji'anHuang ShuaishuaiLiu XinqiMa Biao - Moyamoya disease (MMD) is a chronic, progressive occlusive cerebrovascular disease. It causes recurrent cerebrovascular stroke due to vascular closure and proliferation. An unclear pathophysiological mechanism is the most significant obstacle in the diagnosis and treatment of MMD. - Source: PubMed
Publication date: 2025/07/28
Zhou ZhenyuNiu HongchuanXu ShaoqiZhang JunzeLiu YutongLei ChengxuHe ShihaoZhao Yuanli - Chronic kidney disease (CKD), characterized by gradual loss of renal function, may be driven by environmental exposure such as perfluoroalkyl and polyfluoroalkyl substances (PFAS), yet the intrinsic mechanisms are largely unknown. Here, we observed distinct proteinuria in the mice exposed to sodium -perfluorous nonenoxybenzenesulfonate (OBS), an alternative to perfluorooctanesulfonate. The renal S-adenosylhomocysteine (SAH) level increased due to the decrease in its hydrolase adenosylhomocysteinase (AHCY), and was positively correlated with the observed proteinuria. Consequently, the DNA methylation level was downregulated. Specifically, the promoter methylation of increased, while the genebody methylation of decreased, thereby causing downregulation of their mRNA expressions. This further suppressed the levels of Rho GTPases and , which then reduced their downstream genes , and , and eventually inhibited expression. Consequently, the podocyte cytoskeleton was disrupted, promoting foot process fusion and inducing proteinuria. Overexpression of AHCY in OBS-exposed mice reduced the level of SAH, restored the methylation levels and gene expressions, ameliorated the podocyte injury, and eventually reduced the level of urinary protein. Taken together, inhibition of AHCY was the molecular initiating event of OBS-induced proteinuria, which functioned through the AHCY-SAH-Arap3/Tiam1-RhoA/Rac1-Pip5k1a/Pip5k1b/Pip5k1c-Actn4 axis. This study provides profound insight into the potential risk of PFAS in disrupting renal function and kidney health. - Source: PubMed
Publication date: 2025/05/30
Lyu YangGuo RuyuZhong WenjueZhu Lingyan