Ask about this productRelated genes to: USP42 antibody
- Gene:
- USP42 NIH gene
- Name:
- ubiquitin specific peptidase 42
- Previous symbol:
- -
- Synonyms:
- FLJ12697
- Chromosome:
- 7p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-04
- Date modifiied:
- 2018-11-22
Related products to: USP42 antibody
Related articles to: USP42 antibody
- This study investigated the role of ubiquitin specific peptidase 42 (USP42) in breast cancer proliferation, focusing on its modulation of apoptosis via the JNK/p38 signaling pathway. USP42 expression levels in breast cancer cell lines were assessed using western blotting and RT-qPCR. In vitro, cell proliferation was evaluated using CCK-8 assay and clonogenic assay assessed, while apoptosis was measured by flow cytometry evaluated. Western blotting was used to analyze the expression of apoptosis-related proteins and those associated with the JNK/p38 pathway. The effect of USP42 knockdown on breast cancer cell proliferation was examined in vivo using a xenograft nude mice model. USP42 protein levels were significantly higher in breast cancer tissues than in normal breast tissues. Moreover, USP42 expression was positively correlated with the advanced T stage, N stage, and pathological stage. USP42 knockdown in MCF7 and MDA-MB-231 cells resulted in decreased proliferation and increased apoptosis rates. USP42 silencing upregulated caspase-3 and Bax expression, while downregulating Bcl-2. Phosphorylation of JNK and p38 increased significantly following USP42 silencing. Treatment with SP600125 (JNK inhibitor) or SB203580 (p38 MAPK inhibitor) effectively recused JNK and p38 activation. Both inhibitors also reduced the apoptotic cell population, which was upregulated by USP42 silencing. These findings highlight USP42 promotes breast cancer progression by reducing JNK and p38 activation and inhibiting apoptosis, suggesting its potential as a therapeutic target in breast cancer treatment. - Source: PubMed
Publication date: 2025/10/21
He ChongwuChen JingTian RuiboYang LiuHe WenruiHe LongboXu JiaweiLi JianglongWang GongxianJiang ChanganLiu QiangWan XianghuaYu Tenghua - Fusion genes are major drivers of acute leukemia. Conventional diagnostics are limited in detecting the diverse fusions included in recently updated acute leukemia classifications. We evaluated the fusion detection performance of RNA sequencing (RNA-seq) compared with that of conventional diagnostics in patients with acute leukemia. - Source: PubMed
Publication date: 2025/10/16
Kim Hyun-YoungKim BoramPark Min-SeungPark Jong-HoJu Hee YoungYoo Keon HeeJang Jun HoJung Chul WonKim Hee-Jin - Prostate cancer (PCa) is one of the most common cancers in men worldwide. During its progression, deubiquitination-mediated alterations in biological processes play critical roles in tumor metabolism, stem cell characteristics, immune evasion, DNA damage repair, and chemoresistance. A comprehensive investigation of the deubiquitinases involved in PCa development holds significant clinical value as regards inhibiting tumor growth and overcoming drug resistance. - Source: PubMed
Publication date: 2025/07/11
Zhou YinghaoChen ChenchenMeng YiboGe JianchaoMeng ShengkuiWang XillongXu YaozongShi GuoweiYu WandongHu XuetaoZhang Jun - Liver regeneration is critical for maintaining whole-body homeostasis, especially under exposure to deadly chemical toxins. Understanding the molecular mechanisms underlying liver repair is critical for the development of intervention strategies to treat liver diseases. In this study, ubiquitin-specific Proteases 42 (USP42) is identified as a novel deubiquitinases (DUB) of peroxisome proliferators-activated receptor γ (PPARγ) in hepatocytes. This DUB interacted, deubiquitinated, and stabilized PPARγ, and increased PPARγ targeted proliferative and antioxidative gene expressions, which protects the liver from carbon tetrachloride (CCL4) induced oxidative injury and promotes liver regeneration. In addition, fibroblast growth factor 2 (FGF2) initiated USP42 expression and enhanced the interaction between USP42 and PPARγ during the liver regeneration process. Moreover, the PPARγ full agonist, rosiglitazone (RSG), possesses the ability to further reinforce the USP42-PPARγ interplay, which enlightens to construct of an extracellular vesicle-based targeting strategy to activate the liver USP42-PPARγ axis and promote liver regeneration. In summary, the work uncovers the importance of USP42-PPARγ axis-mediated liver tissue homeostasis and provides a promising regimen to target this protein-protein interplay for liver regeneration. - Source: PubMed
Publication date: 2025/03/17
Yang NanfeiTian QiangLei ZhenliWang ShuxinCheng NanWang ZhenJiang XianqinZheng XuqunXu WenjingYe MinyanZhao LongweiWen MeiyunNiu JianlouSun WeijianShen PingpingHuang ZhifengLi Xiaokun - In a family with Familial Non-Medullary Thyroid Carcinoma (FNMTC), our investigation using Whole-Exome Sequencing (WES) uncovered a novel germline mutation []. USP42 is known for regulating p53, cell cycle arrest, and apoptosis, and for being reported as overexpressed in breast and gastric cancer patients. Recently, a missense mutation was described in FNMTC, suggesting a potential involvement in thyroid cancer. Aiming to explore the mutation as an underlying cause of FNMTC, our team validated the mutation in blood and tissue samples from the family. Using immunohistochemistry, the expression of USP42, Caspase-3, and p53 was assessed. The gene was silenced in human thyroid Nthy-Ori 3-1 cells using siRNAs. Subsequently, expression, viability, and morphological assays were conducted. p53, Cyclin D1, p21, and p27 proteins were evaluated by Western blot. USP42 protein was confirmed in all family members and was found to be overexpressed in tumor samples, along with an increased expression of p53 and cleaved Caspase-3. siRNA-mediated downregulation in Nthy-Ori 3-1 cells resulted in reduced cell viability, morphological changes, and modifications in cell cycle-related proteins. Our results suggest a pivotal role of mutation in thyroid cell biology, and this finding indicates that USP42 may serve as a new putative target in FNMTC. - Source: PubMed
Publication date: 2024/01/26
Teixeira ElisabeteFernandes CláudiaBungărdean MariaPaula Arnaud Da CruzLima Raquel TBatista RuiVinagre JoãoSobrinho-Simões ManuelMáximo ValdemarSoares Paula