Ask about this productRelated genes to: FBXO7 antibody
- Gene:
- FBXO7 NIH gene
- Name:
- F-box protein 7
- Previous symbol:
- -
- Synonyms:
- FBX7, Fbx, PARK15
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-09-27
- Date modifiied:
- 2015-08-25
Related products to: FBXO7 antibody
Related articles to: FBXO7 antibody
- Mutations in the PARK15/FBXO7 gene cause an early-onset parkinsonian syndrome. A mouse with conditional knockout of Fbxo7 in dopaminergic neurons models key features of this pathology, exhibiting a progressive loss of striatal tyrosine hydroxylase (TH)-positive terminals that precedes cell death. This gradual decline in a mammalian model provided an opportunity to test the capacity of Fbxo7 to act as a therapeutic agent and define a treatment window for gene replacement. Using a recombinant adeno-associated virus (rAAV), we delivered Fbxo7 to test its capacity to prevent (delivery prior to deficit onset) and rescue (delivery after nigrostriatal phenotypes were evident) dopaminergic markers. Remarkably, Fbxo7 re-expression rescued DAT and TH-immunoreactivity in the striatum and nucleus accumbens before and after the onset of the loss of TH + staining. These data establish that Fbxo7-dependent neurodegeneration is not an irreversible process, highlighting its regulated pathways as promising potential targets for developing therapies that will not only slow disease progression, but also ameliorate dopaminergic terminal deficits and potentially restore function. - Source: PubMed
Publication date: 2026/04/16
Al Rawi SaraTyers PamelaBarker Roger ALaman Heike - Coexisting myocardial infarction (MI) and type 2 diabetes mellitus (T2DM) is a common condition. We aimed to investigate the association between MI and type 2 diabetes (T2D) with mitophagy-related differentially expressed genes (MRDEGs) and the impact thereof on disease progression. - Source: PubMed
Publication date: 2026/04/08
Yang YingWan FeiyanXu XuelianXu WeiJiang LingliPan Pei - Parkinson's disease (PD) is characterized by mitochondrial dysfunction and impaired protein homeostasis, with the mitochondrial unfolded protein response (mtUPR) emerging as a key regulatory pathway in mitigating mitochondrial stress. This study aimed to explore the impact of shRNAs targeting CHCHD2 or FBXO7 on the mitochondrial unfolded protein response (mtUPR) in a Parkinson's disease (PD) cell model, clarify the mitochondrial-nuclear signaling pathways involving CHCHD2 and FBXO7, elucidate the mechanisms underlying mitochondrial dysfunction induced by these genes, and identify new therapeutic targets for early stage PD. An in vitro PD model was established by treating SH-SY5Y cells with MPP; mitochondrial morphology was evaluated using transmission electron microscopy, and qRT-PCR and Western blot were employed to determine the expression levels of mRNAs and proteins associated with mtUPR, autophagy, CHCHD2, and FBXO7 under oxidative stress. In the MPP-induced PD cell model, we knocked down CHCHD2 and FBXO7 via shRNA and treated the cells with JNK and AKT agonists to observe their effects on mtUPR protein expression. The results showed that mtUPR was activated in MPP-exposed SH-SY5Y cells, and the expression of CHCHD2 and FBXO7 genes was significantly upregulated after MPP intervention; knockdown of CHCHD2 via shRNA resulted in a marked decrease in the expression of mtUPR-related proteins such as HSPA9, HSPD1, YME1L1, and CLPP, while shRNA targeting FBXO7 exerted only a minimal effect on these mtUPR proteins. Furthermore, the administration of JNK or AKT agonists significantly enhanced the expression of MPP-induced mtUPR proteins, including HSPA9, HSPD1, YME1L1, and CLPP. Collectively, these findings indicate that CHCHD2, rather than FBXO7, plays an essential role in modulating the MPP-induced mtUPR and suggest that CHCHD2 may regulate mitochondrial protein homeostasis by activating the mtUPR through the JNK/c-Jun and AKT/ERα pathways. - Source: PubMed
Publication date: 2026/02/05
Wen DongniLi YunjingChen LinaXu HaolingWang YingqingWeng YanhongZhang JingChen XiaochunHuang EnZeng YuqiYe Qinyong - Endothelial dysfunction underlies the pathogenesis of many diseases, including atherosclerosis, diabetes, and kidney failure. The EA.hy926 cell line is one of the most widely used human macrovascular endothelial cell models, and has been shown to enter both dysfunctional- and quiescent-like states. However, there are no validated housekeeping genes (HKGs) for EA.hy926 cells, especially suitable for different growth states and fatty acid treatments. Therefore, we screened transcriptomic data of EA.hy926 cells in their growing and quiescent states and after treatment with or without docosahexaenoic acid (DHA), and identified 18 candidate HKGs. Together with eight other commonly used HKGs and one HKG identified from databases, the stability of the 27 candidate HKGs were analyzed with five algorithms: deltaCt, BestKeeper, geNorm, NormFinder, and RefFinder, using the RT-qPCR results of EA.hy926 cells under 4 different growth conditions. The comprehensive ranking results from RefFinder suggested that the top two most stable genes were and , whereas the least stable commonly used HKGs were and . The suitability of these genes as HKGs for EA.hy926 cells in different growth states and in response to DHA treatment were validated in relation to the expression of selective endothelial markers. The RT-qPCR validation results confirmed that normalization with + provided greater sensitivity than the commonly used HKGs in detecting the expression difference of those endothelial markers under different conditions (growth state × DHA treatment). This novel panel of HKGs is available for future studies of EA.hy926 cell responses to different growth states and/or following DHA treatment. - Source: PubMed
Publication date: 2026/01/20
Huang ShiqiSivakumar Samritha RamanCharney JordanFisher Rachel AkongTaylor Carla GZahradka Peter - Recent studies have shown that heat shock protein 90 alpha family class A member 1 (HSP90AA1) interacts with various tumor-associated proteins, regulates their biological activity and stability, and plays an important role in various tumors. However, the role of HSP90AA1 in clear cell renal cell carcinoma (ccRCC) remains unclear. In the study, GEO and TCGA-KIRC databases were used to analyze the expression pattern and clinical significance of HSP90AA1 in ccRCC; immunohistochemistry and Western blot were used to validate HSP90AA1 expression in ccRCC tissues and cell lines; colony formation assays, EdU and TUNEL methods, cell migration and invasion experiments, and a mouse renal orthotopic xenograft tumor model were used to detect the effects of HSP90AA1 overexpression on the biological function of ccRCC; Co-IP and RNA-seq experiments were utilized to explore the downstream regulatory mechanism of HSP90AA1. Our results showed that HSP90AA1 expression was significantly downregulated in ccRCC, and its reduced expression was associated with tumor metastasis. HSP90AA1 overexpression markedly inhibited the proliferation and metastasis ability of ccRCC cells. HSP90AA1 bound to F-box only protein 7 (FBXO7) and accelerated its protein expression. FBXO7 was expressed at low level in ccRCC, and its decreased expression was closely related to unfavorable pathological features of tumors and poor patient prognosis. FBXO7 overexpression promoted cell adhesion molecule 1 (CADM1) expression and suppressed the PI3K-AKT signaling pathway. Knocking down FBXO7 expression on the basis of HSP90AA1 overexpression significantly reversed the cell phenotype inhibition caused by HSP90AA1 overexpression, downregulated CADM1 expression, and activated the PI3K-AKT signaling pathway. In summary, HSP90AA1 exhibited a low expression pattern in ccRCC, and HSP90AA1 overexpression promoted CADM1 expression and inhibited the PI3K-AKT pathway, thereby suppressing the proliferation and metastasis of ccRCC. - Source: PubMed
Publication date: 2026/01/08
Yang WupingLi YifanLi ZhiJiang ChaochaoDeng XuPeng Ding