Ask about this productRelated genes to: PSME1 antibody
- Gene:
- PSME1 NIH gene
- Name:
- proteasome activator subunit 1
- Previous symbol:
- -
- Synonyms:
- IFI5111, PA28alpha
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 1997-02-11
- Date modifiied:
- 2016-10-05
Related products to: PSME1 antibody
Related articles to: PSME1 antibody
- This study integrates single-cell and bulk RNA-seq to investigate cell type-specific alterations in fatty acid metabolism-related genes in the dorsolateral prefrontal cortex (DLPFC) of schizophrenia (SCZ) patients and to evaluate their potential as diagnostic biomarkers. - Source: PubMed
Publication date: 2026/04/21
Zhao CuiZhang LiangYang PingLi LiangZeng WeiqiXie Weiqi - Pegylated interferon alpha (Peg-IFN-α) has the potential for eradicating hepatitis B surface antigen (HBsAg). The aim of our study is to investigate whether the expression levels of adenosine deaminase acting on RNA 1 (ADAR1), NEDD4-binding protein 1 (N4BP1), proteasome activator complex subunit 1 (PSME1) mRNAs in peripheral blood mononuclear cells (PBMCs) of HBeAg-negative chronic hepatitis B virus (HBV) patients are associated with the response to Peg-IFN-α treatment and HBsAg clearance. - Source: PubMed
Publication date: 2026/04/13
Pang HaoFu XinglinChen LüpingYang ShuhanYang FanQin Bo - To investigate the potential molecular regulatory mechanism of interferon-α (IFN-α)-induced disulfidptosis occurrence in human liver cancer cells. Glucose starvation and IFN-α treatment models were constructed using human hepatocellular carcinoma cell lines HepG2 and Huh7, respectively. Western blotting (WB), NADPH content measurement, and immunofluorescence staining were employed to evaluate disulfidptosis-related phenotypes, such as intracellular disulfide bond accumulation, NADPH depletion, and filamentous actin (F-actin) skeleton collapse. The reversibility of the phenotypes was validated by combining the disulfidptosis inhibitor D-penicillamine (D-Pen). The expression of solute carrier family 7 member 11 (SLC7A11) was downregulated using siRNA interference to evaluate the dependence of IFN-α-induced disulfidptosis on the SLC7A11 pathway. Furthermore, the GEO transcriptome dataset was employed to conduct differential gene analysis for screening candidate molecules involved in the regulation of IFN-α-induced disulfidptosis. Quantitative data are presented as mean ± standard deviation (SD). Comparisons between two groups were performed using the independent-samples test, while comparisons among multiple groups were analyzed by one-way analysis of variance (ANOVA), followed by Dunnett's t test for pairwise comparisons. Compared with the control group, glucose starvation and IFN-α treatment both induced disulfidptosis-related phenotypes in HepG2 and Huh7 cells, characterized by increased intracellular disulfide bond levels, decreased NADPH content, and F-actin cytoskeleton collapse. Following IFN-α treatment, the accumulation of high-molecular-weight protein aggregates increased in a time- and dose-dependent manner. Compared with IFN-α treatment alone, combined D-Pen intervention partially alleviated intracellular disulfide accumulation, NADPH depletion, and F-actin cytoskeletal collapse. Under conditions of SLC7A11 knockdown, IFN-α-induced high-molecular-weight protein aggregation was further aggravated, suggesting that regulatory mechanisms independent of SLC7A11 may also be involved in this process. Transcriptomic differential expression analysis revealed that β2-microglobulin (B2M), ubiquitin-specific peptidase 18 (USP18) and proteasome activator subunit 1 (PSME1) were upregulated following IFN-α stimulation, among which PSME1 also showed increased protein expression after IFN-α treatment. IFN-α can induce disulfidptosis-related phenotypic changes in HepG2 and Huh7 human hepatocellular carcinoma cells. The upregulation of B2M, USP18, and PSME1 suggests that these molecules may be involved in this process; however, the specific underlying mechanisms require further investigation. - Source: PubMed
Bi X YZhang JXu L HChu X RLiu S SXin Y N - Porcine reproductive and respiratory syndrome virus (PRRSV) poses a significant threat to the global swine industry, employing complex mechanisms to interact with the host and evade host immune responses. The ubiquitin-proteasome system (UPS) is central to host antiviral innate immunity, yet its interplay with PRRSV remains poorly understood. In this study, Proteasome 20S Subunit Alpha 2 (PSMA2) was identified as a novel host restriction factor against highly pathogenic PRRSV (HP-PRRSV). Through overexpression and siRNA knockdown experiments, it was demonstrated that PSMA2 effectively inhibits PRRSV replication in a time- and dose-dependent manner, exerting antiviral effects during the mid-to-late post-entry stages of replication. Mechanistically, PSMA2 overexpression enhances overall cellular proteasome activity and specifically upregulates transcription of immunoproteasome activator subunits PSME1, PSME2, and PSME3. As a countermeasure, the PRRSV JXA1 strain induces the degradation of PSMA2 protein via the autophagy pathway, a process contingent on active viral replication. Further screening identified PRRSV nonstructural protein 12 (Nsp12) as a viral factor associated with the autophagy-dependent reduction of PSMA2. In parallel, PRRSV infection suppresses global proteasome activity, indicating that the virus adopts a two-pronged strategy to undermine this host defense pathway. These findings demonstrate that PRRSV hijacks autophagy machinery to eliminate a key proteasome-associated restriction factor. Collectively, our results highlight the intricate interplay between PRRSV and the host proteasome system and provide novel insights into viral pathogenesis. - Source: PubMed
Publication date: 2025/12/10
Li WeiYang DanjiaoWang RuiqingLan LanQiu XinxinWang Xinglong - Analyzing the content of immune cell-derived extracellular vesicles (EVs) may reveal biomarkers that elucidate the mechanisms through which infection negatively affects outcomes in patients with intracerebral hemorrhage (ICH). - Source: PubMed
Publication date: 2025/12/04
Laso-García FernandoAlonso-López ElisaPiniella DoloresDíez-Tejedor ExuperioGómez-de Frutos Mari CarmenCasado-Fernández LauraOtero-Ortega LauraLópez-Molina Mari PazGallego-Ruiz RebecaPozo-Novoa JavierCalzado-González ÁngelaDíaz-Gamero NereaRomán-San Martín AliciaBravo SusanaBarderas RodrigoDocando FélixFuentes BlancaJuárez-Martín BelénAlonso de Leciñana MaríaGutiérrez-Fernández María