Ask about this productRelated genes to: NFATc1 antibody
- Gene:
- NFATC1 NIH gene
- Name:
- nuclear factor of activated T cells 1
- Previous symbol:
- -
- Synonyms:
- NF-ATC, NFATc, NFAT2
- Chromosome:
- 18q23
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-16
- Date modifiied:
- 2017-12-06
Related products to: NFATc1 antibody
Related articles to: NFATc1 antibody
- Acute myeloid leukemia (AML) remains therapeutically challenging, highlighting an urgent need for novel therapeutic targets. Our prior work showed ENO1 promotes AML, but the role of its short variant MBP1 was unknown. Here, we demonstrated significant downregulation of MBP1 alongside ENO1 upregulation in primary AML patient samples compared to healthy donors, establishing an imbalanced ENO1/MBP1 ratio. Functionally, restoring MBP1 expression in AML cell lines (KG1, OCI-AML3) inhibited cell proliferation, suppressed colony formation, induced cell apoptosis, and triggered G1-phase cell cycle arrest . Mechanistically, RNA-seq and pathway analysis revealed that MBP1 overexpression suppresses the non-canonical Wnt/Ca signaling pathway by downregulating its key components Wnt11 and NFATc1. Crucially, studies using NSG mouse xenografts confirmed that MBP1 overexpression significantly attenuated AML progression, reducing tumor burden in spleen and bone marrow. These results demonstrate that MBP1 deficiency promotes AML via Wnt11/NFATc1 activation, revealing a promising therapeutic target. - Source: PubMed
Publication date: 2026/04/23
Gao BeibeiYan WenliXue JingjingZhang ShanshanWang FurongKang ZhijieRen JinhongYan JinsongWang Haina - Osteoporosis is a major skeletal disorder characterized by reduced bone strength and increased risk of fractures. Excessive osteoclast-mediated bone resorption is a primary cause of this condition, underscoring the need for effective anti-resorptive therapies. N-phenyl-methylsulfonamido-acetamide (PMSA) compounds have been previously identified as potential anti-resorptive agents that inhibit osteoclastogenesis. In this study, ribonucleic acid (RNA)-sequencing and proteomic analyses identified calcineurin (CaN) as a potential target of PMSA implicated in osteoclast differentiation. PMSA bound to CaN and suppressed its phosphatase activity, which is essential for the activation and translocation of nuclear factor of activated T cells, cytoplasmic 1 (NFATc1), a key regulator of osteoclastogenesis. PMSA treatment resulted in altered NFATc1-related signaling and increased phospho-NFATc1 levels in osteoclasts. Overall, these findings suggest that PMSA may inhibit CaN activity during osteoclast differentiation, positioning it as a promising therapeutic candidate for osteoporosis. - Source: PubMed
Publication date: 2026/04/22
Cho EunjinCheon SeongminChoi Dong KyuYang Hee-YoungPark ChungooLee Tae-Hoon - - Source: PubMed
Publication date: 2026/04/21
Zhang LishanLv YinpingXian GuozheLin Yanliang - Osteoclast hyperactivity is a key factor in the pathogenesis of several skeletal disorders, includinginflammatory bone loss, periprosthetic osteolysis, and rheumatoid arthritis. The ubiquitin-proteasome system (UPS) is pivotal in bone homeostasis and disease pathogenesis, modulating critical osteogenic and osteolytic signaling cascades. Our study identified Spautin-1, an inhibitor of ubiquitin-specific protease 10 (USP10), with the capacity to suppress osteoclastogenesis and the expression of genes associated with osteoclast activity, triggered by the nuclear factor-κB (NF-κB) ligand (RANKL) in bone marrow-derived macrophages (BMMs). Spautin-1 also effectively inhibited RANKL-induced bone resorption in vitro assays. At the molecular level, Spautin-1 reduced the expression of JNK interacting protein 1 (JIP1) by impeding USP10-mediated JIP1 deubiquitination, consequently dampening the RANKL-activated c-Jun N-terminal kinase (JNK)-mitogen-activated protein kinase (MAPK) signaling axis and curbing nuclear factor of activated T cells 1 (NFATc1) activation. Consistent with this mechanism, silencing of USP10 similarly reduced the expression of osteoclast‑related genes, mirroring the effects observed with Spautin‑1 treatment, whereas overexpression of JIP1 reversed these inhibitory effects. Additionally, Spautin-1 was found to ameliorate lipopolysaccharide (LPS)-induced bone loss in murine models. Notably, a positive correlation was observed between USP10 and JIP1 expression levels in bone tissues from osteoporotic patients. Collectively, our results position Spautin-1 as a potential therapeutic agent for osteoclast-mediated bone diseases. - Source: PubMed
Publication date: 2026/04/20
Chen XinyiXiao YueWu HanZhong MingliangZhong RongdeChen ShaoyingTang HaimeiDi QianqianZhao XibaoGao YuliChen WeiHuang QiChen Weilin - Osteoclast overactivation is a central driver of bone metabolic disorders such as osteoporosis, and novel drug targets for these diseases continue to be actively explored. Scaffold proteins, which enhance the specificity of deubiquitinase (DUB)-substrate interactions, have emerged as promising therapeutic targets for the sustained management of chronic diseases. Intraflagellar transport (IFT) proteins, recognized for their scaffolding roles in cellular signaling, are increasingly implicated in bone remodeling. However, their therapeutic potential for bone metabolic disorders remains to be fully elucidated. - Source: PubMed
Publication date: 2026/04/02
Gao YuanLai BowenYan RanHe JinnanLu TingweiYang ShiyuanChen JunGao RuiJiang HengZhou Xuhui