CUL3 Antibody
- Known as:
- CUL3 Antibody
- Catalog number:
- 32149
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- CUL3 Antibody
Related genes to: CUL3 Antibody
- Gene:
- CUL3 NIH gene
- Name:
- cullin 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q36.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-29
- Date modifiied:
- 2014-11-19
Related products to: CUL3 Antibody
Related articles to: CUL3 Antibody
- Oxeiptosis is a ROS-induced, caspase-independent form of regulated cell death, but its role in osteoarthritis (OA) remains largely unexplored. This study aimed to identify oxeiptosis-associated molecular markers in OA synovium and establish an oxeiptosis-based molecular classification system. This study integrated five publicly available GEO datasets for comprehensive analysis. GSE55235 and GSE55457 were used as discovery cohorts to identify DEGs between OA and normal synovial tissues. The GSE206848 dataset was utilized to perform correlation analysis with the key oxeiptosis regulators, including , , , and , thereby establishing an oxeiptosis-associated gene set. These genes were intersected with OA-related DEGs to obtain ORDEGs. Subsequently, LASSO regression, SVM-RFE, and RF algorithms were jointly applied to identify hub differential genes. Based on the identified oxeiptosis-related feature genes, molecular subtypes of OA were constructed, with the GSE46750 dataset used for machine learning-based feature selection. Consensus clustering was then performed based on the selected features to identify distinct OA molecular subtypes. The immune microenvironment characteristics and potential regulatory networks of different subtypes were further investigated using CIBERSORT, ESTIMATE, and WGCNA. Finally, an independent GSE89408 cohort was employed for external validation. A total of 159 common differentially expressed genes were identified from the two OA synovial cohorts, which were mainly enriched in cellular response to hydrogen peroxide, the MAPK signaling pathway, the PI3K-Akt signaling pathway, and NF-κB-related inflammatory processes. Further screening identified seven ORDEGs, including , , , , , , and . Machine learning analysis ultimately identified and as potential molecular features of OA. Molecular clustering based on oxeiptosis-related features demonstrated that OA samples could be stably classified into two subtypes, C1 and C2. The C2 subtype exhibited higher ORDEG scores, increased expression levels, greater M1 macrophage infiltration, and higher ESTIMATE scores, indicating oxidative stress-related transcriptional characteristics and enhanced inflammatory features, whereas was mainly highly expressed in the C1 subtype. WGCNA further revealed that the salmon module closely associated with the C2 subtype was mainly enriched in calcium signaling, focal adhesion, cytoskeletal remodeling, and cell adhesion-related pathways. In the independent GSE89408 validation cohort, exploratory clustering analysis again identified two potential molecular subtypes, and remained significantly differentially expressed between the two subtypes. In addition, and showed AUC values of 0.735 and 0.647, respectively, for distinguishing OA from normal synovial tissues. This study establishes an oxeiptosis-associated molecular subtyping framework for OA synovium and identifies and as candidate oxeiptosis-associated genes. Further analyses revealed distinct immune microenvironment characteristics and transcriptional regulatory patterns associated with different oxeiptosis states. External validation provided partial support for the reproducibility of these molecular patterns, particularly the -related features. These findings provide transcriptomic evidence for exploring molecular heterogeneity in OA and generate hypotheses for future mechanistic and clinical validation studies. - Source: PubMed
Publication date: 2026/09/16
Huang HuiwenChen XuwuSun WenxiaLan XiyanZeng ZhiyiLiu YushangYin AnDeng QiongZhong YanbiaoWang Maoyuan - The tumor microenvironment (TME) domesticates macrophage function by decreasing chromatin accessibility. The activation and nuclear translocation of ATP-citrate lyase (ACLY) convert citrate to acetyl-CoA, providing a substrate necessary for histone acetylation. However, the underlying mechanisms in macrophage remodeling are poorly understood. Here, we found that saturated fatty acids (sFA), especially palmitic acid (PA), were lower in TAMs of patients with hepatocellular carcinoma (HCC). Scd1 knockout promoted PA accumulation, resulting in both primary and metastatic liver cancer retardation and overall survival improvement. Mechanisms indicated that ACLY-C893 palmitoylation via PA maintained tetramer stability against CUL3-mediated degradation, facilitating histone acetylation of M1-related genes. Notably, both dietary PA with Scd1 macrophage infusion and TAM-targeted in vivo PA/shSCD1 reprogramming improved the TME to repress HCC progression. Collectively, our research highlights the crucial role of ACLY palmitoylation in the connection between macrophage FA metabolism and histone acetylation reprogramming, which sheds light on the strategy of macrophage-based HCC immunotherapy. - Source: PubMed
Publication date: 2026/09/03
Zhao JunlongXie DongkunSi JingwenFan FanGao ChunchenYang ZhiweiYu HengchaoZhang HuanHu YiyangWang LiangCao XiuliLiang ShiqianCheng ShilinFeng LanGuan FengZhao XiaodiShang LeiNie YongzhanLiu LeiQin Hongyan - Chronic kidney disease (CKD) is characterized by proximal tubule (PT) stress, oxidative injury, and metabolic dysfunction. Human kidney single-nucleus RNA-sequencing (snRNA-seq) identified enrichment of ubiquitin-dependent protein catabolic processes in injured PT cells, suggesting activation of the ubiquitin-proteasome system during tubular stress. Because Cullin 3 (CUL3), scaffold of ubiquitin ligases, regulates oxidative stress signaling through the KEAP1-NRF2 axis, we investigated its role in PT injury and stress adaptation. - Source: PubMed
Publication date: 2026/09/02
Saritas TurgayChen LuIjaz SadafZiegler SusanneDugourd AurélienShao XiaohangUlrich JonathanKoenig ClaireFranciosa GiuliaPiga IlariaOlsen Jesper VSchneider-Kramann RebekkaMcCormick James AHayat SikanderKramann Rafael - Potassium channel tetramerization domain-containing protein 17 (KCTD17) is part of the BTB/POZ domain-containing KCTD protein family and serves as a multifunctional regulator of cellular homeostasis. As an adaptor protein associated with Cullin 3 (CUL3)-based E3 ubiquitin ligase complexes, KCTD17 plays a critical role in selective protein ubiquitination and proteasomal degradation, influencing the stability of various cellular proteins. This function links KCTD17 to numerous biological processes, including organelle dynamics, cell differentiation, intracellular signaling, metabolic regulation, stress responses, tissue remodeling, and disease progression. Notably, the effects of KCTD17 are highly context-dependent, varying with cell type, substrate availability, and pathological conditions. While recent studies have begun to uncover several pathways associated with KCTD17, its complete range of substrates, regulatory mechanisms, and physiological significance are still not fully understood. In this review, we summarize the current understanding of KCTD17's molecular functions and biological mechanisms, emphasizing its role as a proteostatic regulator. We also explore its potential relevance to human diseases and highlight key unresolved questions, such as substrate specificity, tissue-dependent functions, functional redundancy with related KCTD proteins, and therapeutic potential. Gaining a deeper understanding of KCTD17-dependent protein regulation may offer new insights into proteostasismediated cellular regulation and disease mechanisms. - Source: PubMed
Publication date: 2026/09/02
Jeong YelinGi HyunJoonJung Young HoonOh Ah-ReumKim Do-WanKim Young UnChoi Young DuKim KyeongJin - The simultaneous modulation of oxidative stress and autophagy represents a potential therapeutic strategy for amyotrophic lateral sclerosis (ALS), yet agents capable of coordinately regulating both processes remain scarce. The Keap1‑Nrf2‑ARE pathway serves as a critical hub linking redox homeostasis and autophagic regulation, making it an attractive target for ALS intervention. JWA is a stress‑responsive protein involved in cellular protection against oxidative injury, and its neuroprotective effects have been shown to depend on activation of the MEK/ERK‑Nrf2 axis. JP1 is a functional oligopeptide derived from the JWA protein that has been engineered to cross the blood-brain barrier and specifically target integrin αVβ3. Based on the link between JWA and Nrf2 signaling, we hypothesized that JP1 activates the Keap1‑Nrf2‑ARE pathway to coordinate antioxidant defense and autophagic clearance. Here, we evaluated this hypothesis in the SOD1‑G93A mouse model, a well‑established transgenic model of familial ALS, and elucidated the underlying mechanisms. - Source: PubMed
Publication date: 2026/08/25
Zhang YuLiu YaxiShi ShiyuLi QingyangHuo YaniYou PanShu MingzhuCheng XiZhang JunLiang DongZhang AihuaLu ChaoShen BinZhou JianweiNiu Qi