Ask about this productRelated genes to: COMMD8 Blocking Peptide
- Gene:
- COMMD8 NIH gene
- Name:
- COMM domain containing 8
- Previous symbol:
- -
- Synonyms:
- FLJ20502
- Chromosome:
- 4p12
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-13
- Date modifiied:
- 2014-11-19
Related products to: COMMD8 Blocking Peptide
Related articles to: COMMD8 Blocking Peptide
- The COMMD (copper metabolism MURR1 domain-containing) protein family, characterized by a conserved COMM domain, plays crucial roles in metal ion transport and NF-κB signaling regulation in vertebrates. However, its functional roles in invertebrates, particularly crustaceans, remain poorly understood. This study aimed to identify and characterize COMMD family genes in red swamp crayfish (Procambarus clarkii) and to investigate their involvement in immune responses under environmental stress. - Source: PubMed
Publication date: 2025/11/13
Zhang XinCai XiuhongYue ShiruiChen ZhangxuanSun YulongWang Shunchang - The epigenetic modifier N6-methyladenosine (m6A), recognized as the most prevalent internal modification in messenger RNA (mRNA), has recently emerged as a pivotal player in immune regulation. Its dysregulation has been implicated in the pathogenesis of various autoimmune conditions. However, the implications of m6A modification within the immune microenvironment of Sjögren's syndrome (SS), a chronic autoimmune disorder characterized by exocrine gland dysfunction, remain unexplored. Herein, we leverage an integrative analysis combining public database resources and novel sequencing data to investigate the expression profiles of m6A regulatory genes in SS. Our cohort comprised 220 patients diagnosed with SS and 62 healthy individuals, enabling a comprehensive evaluation of peripheral blood at the transcriptomic level. We report a significant association between SS and altered expression of key m6A regulators, with these changes closely tied to the activation of CD4 T cells. Employing a random forest (RF) algorithm, we identified crucial genes contributing to the disease phenotype, which facilitated the development of a robust diagnostic model via multivariate logistic regression analysis. Further, unsupervised clustering revealed two distinct m6A modification patterns, which were significantly associated with variations in immunocyte infiltration, immune response activity, and biological function enrichment in SS. Subsequently, we proceeded with a screening process aimed at identifying genes that were differentially expressed (DEGs) between the two groups distinguished by m6A modification. Leveraging these DEGs, we employed weight gene co-expression network analysis (WGCNA) to uncover sets of genes that exhibited strong co-variance and hub genes that were closely linked to m6A modification. Through rigorous analysis, we identified three critical m6A regulators - , , and - alongside two m6A-related hub genes, and . These elements collectively underscore a complex but discernible pattern of m6A modification that appears to be integrally linked with SS's pathogenesis. Our findings not only illuminate the significant correlation between m6A modification and the immune microenvironment in SS but also lay the groundwork for a deeper understanding of m6A regulatory mechanisms. More importantly, the identification of these key regulators and hub genes opens new avenues for the diagnosis and treatment of SS, presenting potential targets for therapeutic intervention. - Source: PubMed
Publication date: 2024/03/29
Yin JunhaoFu JiayaoXu JiabaoChen ChangyuZhu HanyiWang BaoliYu ChuangqiYang XiujuanCai RuiyuLi MengyangJi KaihanWu WanningZhao YijieZheng ZhanglongPu YipingZheng Lingyan - Celastrol, a bioactive molecule extracted from the plant, has been shown to exhibit anti-inflammatory properties. However, its mechanism of action has not been fully elucidated. Here, we show that celastrol suppresses humoral immune responses and autoimmunity by disabling a protein complex consisting of copper metabolism MURR1 domain-containing (COMMD) 3 and COMMD8 (COMMD3/8 complex), a signaling adaptor for chemoattractant receptors. Having demonstrated the involvement of the COMMD3/8 complex in a mouse model of rheumatoid arthritis, we identified celastrol as a compound that covalently bound to and dissociated the COMMD3/8 complex. Celastrol inhibited B cell migration, reduced antibody responses, and blocked arthritis progression, recapitulating deficiency of the COMMD3/8 complex. These effects of celastrol were abolished in mice expressing a celastrol-resistant mutant of the COMMD3/8 complex. These findings establish that celastrol exerts immunosuppressive activity by targeting the COMMD3/8 complex. Our study suggests that the COMMD3/8 complex is a potentially druggable target in autoimmune diseases and points to celastrol as a lead pharmacologic candidate in this capacity. - Source: PubMed
Publication date: 2023/03/31
Shirai TaiichiroNakai AkikoAndo EmikoFujimoto JunLeach SarahArimori TakaoHigo Daisukevan Eerden Floris JTulyeu JanyerkyeLiu Yu-ChenOkuzaki DaisukeMurayama Masanori AMiyata HaruhikoNunomura KazutoLin BangzhongTani AkiyoshiKumanogoh AtsushiIkawa MasahitoWing James BStandley Daron MTakagi JunichiSuzuki Kazuhiro - Hepatitis B virus (HBV) X protein (HBx) is a viral regulatory and multifunctional protein. It is well-known that the canonical HBx reading frame bears two phylogenetically conserved internal in-frame translational initiation codons at Met2 and Met3, thus possibly generating divergent N-terminal smaller isoforms during translation. Here, we demonstrate that the three distinct HBx isoforms are generated from the ectopically expressed HBV HBx gene, named XF (full-length), XM (medium-length), and XS (short-length); they display different subcellular localizations when expressed individually in cultured hepatoma cells. Particularly, the smallest HBx isoform, XS, displayed a predominantly cytoplasmic localization. To study HBx proteins during viral replication, we performed site-directed mutagenesis to target the individual or combinatorial expression of the HBx isoforms within the HBV viral backbone (full viral genome). Our results indicate that of all HBx isoforms, only the smallest HBx isoform, XS, can restore WT levels of HBV replication, and bind to the viral mini chromosome, thereby establishing an active chromatin state, highlighting its crucial activities during HBV replication. Intriguingly, we found that sequences of HBV HBx genotype H are devoid of the conserved Met3 position, and therefore HBV genotype H infection is naturally silent for the expression of the HBx XS isoform. Finally, we found that the HBx XM (medium-length) isoform shares significant sequence similarity with the N-terminus domain of the COMMD8 protein, a member of the copper metabolism MURR1 domain-containing (COMMD) protein family. This novel finding might facilitate studies on the phylogenetic origin of the HBV X protein. The identification and functional characterization of its isoforms will shift the paradigm by changing the concept of HBx from being a unique, canonical, and multifunctional protein toward the occurrence of different HBx isoforms, carrying out different overlapping functions at different subcellular localizations during HBV genome replication. Significantly, our current work unveils new crucial HBV targets to study for potential antiviral research, and human virus pathogenesis. - Source: PubMed
Publication date: 2021/11/16
Hernández SergioÁlvarez-Astudillo FranciscaGarrido DanielPrieto CristianLoyola AlejandraVillanueva Rodrigo A - Allergen-specific immunotherapy (AIT) is the core treatment in allergic rhinitis and asthma. Although widely used, some patients do not benefit from treatment and there is no efficacy objective marker. - Source: PubMed
Publication date: 2021/09/17
Romantowski JanMaciejewska AgnieszkaPolanska JoannaWasilewska ElizaSpecjalski KrzysztofChełminska MartaJassem EwaNiedoszytko Marek