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
- 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 - Breast cancer and depression are both serious diseases that significantly impact women's physical health. The molecular mechanisms underlying their comorbidity remain elusive. This study aims to identify key genes and the molecular mechanisms associated with the comorbidity of breast cancer and depression using bioinformatics analysis methods. - Source: PubMed
Publication date: 2025/10/17
Xie HuaDing ChenxiangLi QianwenXu JieSheng WeiFeng RenjianCheng Huaidong