RNF178 Blocking Peptide
- Known as:
- RNF178 Blocking Peptide
- Catalog number:
- 33r-10283
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- RNF178 Blocking Peptide
Related genes to: RNF178 Blocking Peptide
- Gene:
- MARCH8 NIH gene
- Name:
- membrane associated ring-CH-type finger 8
- Previous symbol:
- MIR
- Synonyms:
- c-MIR, CMIR, MARCH-VIII, RNF178
- Chromosome:
- 10q11.21-q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-12
- Date modifiied:
- 2018-02-13
Related products to: RNF178 Blocking Peptide
Related articles to: RNF178 Blocking Peptide
- Endothelial cells under oxidative stress and inflammation are vital contributors to the progression of atherosclerosis. Although Orientin possesses antioxidant and anti-inflammatory activities, the effects of Orientin on oxidized low-density lipoprotein and high glucose (ox-LDL/HG)-triggered endothelial cell injury and diabetes-accelerated atherosclerosis remain unclear. ApoE mice were administered streptozotocin (STZ), fed with high-fat diet (HFD), and then treated with Orientin to test the efficacy of Orientin on ameliorating atherosclerosis through pathological and biochemical assays. Human aortic endothelial cells (HAECs) were stimulated by ox-LDL/HG followed by Orientin treatment, and the effects of Orientin on regulating HAEC viability, oxidative stress, inflammation, and endothelial-mesenchymal transition (EndMT) were assessed using cell counting kit-8 (CCK-8), fluorescein diacetate (FDA) staining, quantitative real-time PCR, immunofluorescence (IF), and western blot assays. The results showed that Orientin treatment decreased atherosclerotic plaque burden, lipid lesion, and collagen content in aortic and femoral arteries in diabetic mice. Meanwhile, Orientin alleviated hypercholesterolemia, as evidenced by decreased levels of total cholesterol, LDL-cholesterol, and triglyceride. In HAECs, Orientin treatment increased cell viability and decreased inflammation, oxidative stress, and EndMT induced by ox-LDL/HG. Furthermore, Orientin significantly inhibited reactive oxygen species (ROS)-triggered NOD-like receptor family pyrin domain containing 3 (NLRP3) inflammasome activation and pyroptosis, as suggested by cleavage of caspase-1 and gasdermin-D (GSDMD), generation of interleukin (IL)-18 and IL-1β, and lactate dehydrogenase (LDH) release. Mechanistically, Orientin increased E3 ubiquitin ligase membrane-associated RING-CH 8 (MARCH8) expression in HAECs and resulted in subsequent MARCH8-mediated ubiquitination and proteasomal degradation of the NLRP3 protein. Taken together, these data demonstrate that Orientin, which alleviates HAEC inflammation and pyroptosis through regulating the MARCH8/NLRP3 axis, might be a potential candidate for treating diabetes-accelerated atherosclerosis. - Source: PubMed
Li QiGao MinZhong NiZhang Liang-RongZhu Mei-DongGe Wei-JingWang Qian-ZhuChen XinZhang LeiSong Fu-ChenLu Han-Zhi - Dendritic cells (DCs) are crucial antigen-presenting cells that mediate the interplay between innate and adaptive immunity during lethal infections. Here, we report the key role of reticulophagy regulator 1 (RETREG1), a selective autophagy receptor, in maintaining DC maturation and function in the early stage of sepsis. Mechanistically, activating transcription factor 6 (ATF6) acts as a direct transcription factor regulating RETREG1 expression in response to bacterial lipopolysaccharide-induced endoplasmic reticulum (ER) stress. RETREG1-mediated reticulophagy reduces excessive ER stress via the eukaryotic translation initiation factor 2 alpha kinase 3 (EIF2AK3) signaling pathway and inhibits membrane-associated RING-CH-type finger 8 (MARCH8)-dependent major histocompatibility complex class II (MHC-II) ubiquitination to maintain antigen presentation in DCs. Consequently, Cd11cRetreg1, Retreg1, and Atf6 mice exhibit impaired DC function, leading to immunosuppression and multiple organ failure in experimental sepsis. Exploration of samples from septic patients, combined with single-cell bioinformatics analysis, further suggests that a deficit in reticulophagy in DCs is associated with the development of human sepsis. - Source: PubMed
Publication date: 2026/03/24
Yao Ren-QiRen ChaoZheng Li-YuLi Jing-YanWu Wen-FengLi Yu-XuanWang Li-XueDuan YuWang LuLiu Shuang-QingHe Peng-YiZhao Peng-YueTong SenLi Zhi-XuanZhang TuoWu Meng-YaoWei Shu-TingDong NingWu YaoZhang HuiZhu Xiao-MeiZhang Zi-ChengWu Guo-ShengXia Zhao-FanDu Xiao-HuiKang Hong-JunZou ZuiTang Dao-LinYao Yong-Ming - Emerging evidence suggests a crucial role of MARCH8, a membrane-associated RING-E3 ubiquitin ligase, in cancer progression by regulating the turnover of cancer-related proteins. Our previous research identified potential MARCH8 targets using an RNAi-coupled proteomics approach, revealing that MARCH8 mediates the proteasomal degradation of E-cadherin and β2m, contributing to Esophageal Squamous Cell Carcinoma (ESCC) progression. Additionally, EpCAM emerged as a key target, and this study aims to investigate how MARCH8 regulates EpCAM stability and its implications in tumor migration. Herein, Co-immunoprecipitation (Co-IP) and Western Blotting (WB) demonstrated that MARCH8 directly interacts with EpCAM and regulates its turnover by ubiquitination and proteasomal degradation. Further, MARCH8-EpCAM co-localization was observed in ESCC cells using Immunofluorescence (IF). Additionally, Immunohistochemistry (IHC) analysis in ESCC tissues revealed a significant inverse correlation between MARCH8 and EpCAM expression (r = -0.6730, p < 0.0001). Interestingly, EpCAM showed a context-dependent expression in esophageal tissues. Adjacent non-malignant esophageal squamous epithelium showed no detectable EpCAM staining, superficial tumor regions displayed membranous EpCAM expression, whereas tumor cells at the deeper invasive front exhibited markedly reduced or lost EpCAM expression. Consistently, scratch assay coupled with IF and IHC analysis further demonstrated reduced EpCAM expression in migrating ESCC cells. Overexpression studies further revealed an inverse relationship between MARCH8 and EpCAM in migration, invasion, and β-catenin signaling, as shown by invasion/migration assays and WB analysis. Collectively, these findings establish EpCAM as a novel target of MARCH8. Given that loss of EpCAM is associated with migratory phenotypes and that MARCH8 promotes ESCC progression, MARCH8-driven EpCAM degradation may contribute to enhanced tumor cell migration and disease progression. - Source: PubMed
Publication date: 2026/03/23
Bano ArjumandSaraya AnoopDas PrasenjitGunjan DeepakDash Nihar RanjanSharma Rinu - The Membrane-Associated RING-CH (MARCH) family of E3 ubiquitin ligases modulates membrane protein stability and contributes to host antiviral immune responses. Their functions largely depend on the nature of protein substrates. In this study, we identified interferon-induced transmembrane protein 3 (IFITM3), a critical antiviral effector protein, as a novel substrate of MARCH8 by coimmunoprecipitation coupled with LC-MS/MS analysis. Mechanistically, MARCH8 promotes the lysosomal degradation of IFITM3 primarily through K63-linked polyubiquitination at lysine 24, which facilitates its trafficking and turnover from the plasma membrane to endosomes and lysosomes. MARCH8-KO cells exhibit plasma membrane accumulation of IFITM3 compared with WT controls after interferon treatment. Functionally, MARCH8 expression attenuated the IFITM3-mediated restriction of vesicular stomatitis virus and influenza A virus entry, thereby increasing cell susceptibility to viral infection. Together, these findings establish a novel regulatory mechanism whereby MARCH8 modulates innate immunity through regulating the trafficking and turnover of antiviral protein IFITM3. - Source: PubMed
Publication date: 2025/11/04
Wei LiangZhao FeiLiu XiaomanMei ShanHuang YuXie YuHu YameiWang LimingWang LingwaGao ZhaoChen ChenShi YueyueHe YurongWang JiaxunXue TiffanyXu FengwenFang JugaoGuo Fei - Several autonomous mechanisms regulate protein expression, such as transcription, translation, post-translational modifications, and epigenetic changes. Rarely, these processes are controlled by the same molecular player with overlapping roles. Here, we reveal that transcription factor NFATc1 regulates both transcription and degradation of the Ca channel Orai3 in a context-dependent manner. We demonstrate that NFATc1 drives Orai3 transcription in non-metastatic pancreatic cancer cells. In invasive and metastatic pancreatic cancer cells, NFATc1 induces Orai3 lysosomal degradation by transcriptionally enhancing MARCH8 E3-ubiquitin ligase. We show that MARCH8 physically interacts with Orai3 intracellular loop eventually resulting in its ubiquitination at the N-terminal. Mechanistically, the dichotomy in the regulation of Orai3 expression emerges from the differences in MARCH8 epigenetic landscape. We uncover that MARCH8 promoter is hyper-methylated in non-metastatic cells. Importantly, we demonstrate that MARCH8 restricts pancreatic cancer metastasis by targeting Orai3 degradation, thereby highlighting the pathophysiological importance of this signaling module. Taken together, we report a unique and clinically relevant scenario wherein the same transcription factor both enhances and curtails the expression of a target protein in cancer. - Source: PubMed
Publication date: 2025/09/29
Raju SharonSharma AkshayDahiya SakshiRanjan GyanMotiani Rajender K