Porcine beta-arrestin 2,ARRB2 ELISA Kit
- Known as:
- Porcine b-arrestin 2,ARRB2 Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- YHB0046Po
- Product Quantity:
- 48T
- Category:
- Elisa Kits
- Supplier:
- yehua
- Gene target:
- Porcine beta-arrestin 2 ARRB2 ELISA Kit
Related genes to: Porcine beta-arrestin 2,ARRB2 ELISA Kit
- Gene:
- ARRB2 NIH gene
- Name:
- arrestin beta 2
- Previous symbol:
- ARR2
- Synonyms:
- BARR2, DKFZp686L0365
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-10
- Date modifiied:
- 2016-10-05
Related products to: Porcine beta-arrestin 2,ARRB2 ELISA Kit
Related articles to: Porcine beta-arrestin 2,ARRB2 ELISA Kit
- Urate transporter 1 (URAT1, encoded by SLC22A12) is a key mediator of renal urate reabsorption and an important pharmacological target for urate-related disorders. Sodium butyrate (BuNa), a gut microbiota derived short-chain fatty acid, has been implicated in host metabolic regulation, but its role in renal urate transport remains unclear. Here, using molecular docking, cellular thermal shift assays, immunoprecipitation-mass spectrometry and multi-omics analyses, we identified free fatty acid receptor 2 (FFAR2) as a direct target of BuNa in renal proximal tubular HK2 cells . BuNa binding upregulated FFAR2 and promoted URAT1 expression and urate uptake via an FFAR2-dependent pathway. Mechanistically, BuNa/FFAR2 signaling acts via GNAQ to activate PLCβ, generating diacylglycerol and engaging a PKC-dependent p38 MAPK/ELK1 cascade that upregulates arrestin beta 2 (ARRB2). ARRB2 directly binds to IκB, preventing its phosphorylation-dependent degradation, thereby stabilizing IκB and inhibiting NF-κB nuclear translocation. Within the SLC22A12 promoter, NF-κB (RELA/p50) and hepatocyte nuclear factor 1 beta (HNF1β) compete for overlapping binding sites. By blocking NF-κB nuclear entry, BuNa relieves this competition, permitting HNF1β-driven SLC22A12 transcription. Thus, BuNa enhances URAT1-mediated urate reabsorption in HK2 cells via an FFAR2/GNAQ/p38 MAPK/ELK1/ARRB2 axis that stabilizes IκB, suppresses NF-κB, and relieves the competitive binding between NF-κB and HNF1β on the SLC22A12 promoter. These findings establish a previously unrecognized gut microbiota-kidney axis linking microbial BuNa to renal urate homeostasis through a novel transcriptional regulatory circuit. - Source: PubMed
Publication date: 2026/08/03
Cao ChengSun MubinLi JiabaoYuan ZhenyuGu YuweiShao YufanWang LishengJin XiaohuaCheng YijieFan Bo - Glioblastoma (GBM) is among the malignant tumors with the lowest five-year survival rate. Current treatments offer limited efficacy and first-line options are scarce, highlighting the urgent need for novel drugs. Cariprazine can cross the blood-brain barrier and has been reported to inhibit certain tumors; however, its effect on GBM remains unknown. This study aims to elucidate its anti-GBM effects and mechanisms. Cell proliferation and apoptosis were assessed by wound healing, Transwell, colony formation assays, flow cytometry and JC-10 staining. Co-immunoprecipitation (Co-IP) examined the effect of cariprazine on D2/D3-ARRB2 interaction. Direct binding of cariprazine to ARRB2 was determined by molecular docking and CETSA. Western blotting and immunofluorescence detected changes in proliferation and apoptosis-related proteins. In vivo anti-GBM activity was evaluated in subcutaneous mouse models. Cariprazine inhibited GBM cell proliferation and migration, promoted apoptosis, and showed low astrocyte toxicity. In mice, it suppressed GBM allograft growth without overt systemic toxicity. These effects were mediated through D2/D3 receptors, as cariprazine disrupted the D2/D3-ARRB2 interaction and thereby inhibited ERK signaling. It also upregulated ARRB2, further inhibiting the growth of GBM. Molecular docking and CETSA confirmed the direct binding of cariprazine to ARRB2 at LEU-245 and PHE-246. This study is the first to repurpose cariprazine for GBM, elucidating a unique ARRB2-centered dual mechanism, thus offering a new therapeutic strategy. - Source: PubMed
Publication date: 2026/06/12
Zhang HaotianLiu HaoweiXu JiangpengLi XiaolingLi ShashaLiu XuemeiHu Changhua - Periodontitis, a common chronic inflammatory disease, causes connective tissue degradation, alveolar bone resorption, and tooth loss. G protein coupled receptor class C group 5 member A (GPRC5A) regulates chronic inflammation in several diseases, but its role in periodontitis remains unclear. This study investigated GPRC5A expression and function in periodontitis. In human tissues, GPRC5A expression was assessed by immunohistochemistry and quantitative real-time PCR (qRT-PCR). In vivo, adeno associated virus (AAV) mediated GPRC5A silencing was applied in a murine periodontitis model. In vitro, mechanistic studies used small interfering RNA (siRNA) knockdown, co-immunoprecipitation (Co-IP), mass spectrometry, and western blot in periodontal ligament cells (PDLCs). GPRC5A was upregulated in inflamed periodontal tissues, and its downregulation reduced alveolar bone loss and periodontitis severity in mice. GPRC5A knockdown suppressed inflammatory cytokine production and NF-κB activation in lipopolysaccharide (LPS) stimulated PDLCs. β-arrestin 2 (ARRB2) expression paralleled GPRC5A changes, and mass spectrometry/Co-IP identified eukaryotic elongation factor 2 (EEF2) as an ARRB2 binding partner. GPRC5A silencing reduced LPS induced ARRB2 expression and EEF2 phosphorylation. These data suggest a possible mechanistic link that GPRC5A downregulation mitigates periodontitis through the ARRB2‑EEF2 pathway, though direct evidence of causality is still needed. - Source: PubMed
Publication date: 2026/06/11
Hu YuhanLiu RunxuanChen XinxiaoShang Lingling - Precise spatiotemporal regulation of parathyroid hormone (PTH) and PTH-related peptide signaling through the parathyroid hormone receptor 1 (PTH1R) is fundamental to skeletal development and metabolic bone remodeling, yet the intracellular mechanisms that fine-tune this signaling remain a central unanswered question. Here, we identify neurofibromin 2 (Nf2) as an essential regulator of PTH1R trafficking and signaling. Conditional knockout of in chondrocytes results in short-limbed dwarfism, disrupted growth plate organization, and suppressed chondrocyte proliferation and hypertrophy, and a paradoxical bone phenotype marked by trabecular hyperproliferation and cortical thinning. Mechanistically, Nf2 binds to the PTH1R C-terminal domain (464-591 aa) to promote selective receptor internalization via β-arrestin2 without altering G protein-coupled receptor kinase-mediated PTH1R phosphorylation. Loss of decouples PTH1R from β-arrestin2-mediated endocytosis, leading to sustained and amplified signaling through the cAMP-CREB-pSOX9 (S181) and VEGF axis. Consequently, -deficient mice exhibited bone changes similar to those induced by the PTH1R agonist abaloparatide. These findings establish Nf2 as a chondrocyte-intrinsic gatekeeper of PTH1R signaling and uncover a cellular mechanism for bone homeostasis by targeting Nf2-mediated β-arrestin2 recruitment. - Source: PubMed
Publication date: 2026/06/10
Liao JunguangHe YiliangZhang ChenyangQian QitaoHuang YupingZhang QiShen PanpanZhou ChenheWu MengruiChen Guiqian - Altered detection and preference for sodium are associated with increased sodium intake, and increased sodium intake is associated with increased risk of hypertension. ATR (angiotensin II type 1 receptor) second-messenger signaling is mediated and modulated by ARRB2 (β-arrestin-2), and both ATR and ARRB2 in the brain influence sodium intake. Here, we examined the hypotheses that ARRB2 influences sodium taste hedonics and that these effects involve ATR. - Source: PubMed
Publication date: 2026/06/01
Grobe Connie CHamilton Autumn JTreesukosol YadaGrobe Justin LSegar Jeffrey LSigmund Curt D