Ask about this productRelated genes to: ZFP90 antibody
- Gene:
- ZFP90 NIH gene
- Name:
- ZFP90 zinc finger protein
- Previous symbol:
- -
- Synonyms:
- KIAA1954, NK10, ZNF756
- Chromosome:
- 16q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-07
- Date modifiied:
- 2018-11-22
Related products to: ZFP90 antibody
Related articles to: ZFP90 antibody
- Metabolic dysfunction-associated steatotic liver disease (MASLD) has become increasingly common, a trend driven by obesity, excess nutritional intake, and dysfunctional adipose tissue. While continuous dietary stress triggers adipose-tissue-derived lipotoxicity and disrupts hepatic metabolic homeostasis and provokes inflammation, the transcriptional scaffolds that mitigate this lipotoxicity remain incompletely understood. We investigated the role of zinc finger protein 90 (ZFP90) in defending against diet-induced metabolic stress and MASLD pathogenesis. Wild-type and ZFP90-knockout mice were subjected to a high-fat diet (HFD) to model nutrient-overload-induced MASLD. Hepatic phenotypes were characterized using metabolic profiling and RNA sequencing. Mechanistic dynamics were evaluated through protein interaction assays, and clinical relevance was validated using human MASLD liver biopsies. ZFP90 deficiency significantly accelerated HFD-induced steatosis, systemic insulin resistance, and inflammatory infiltration. Crucially, ZFP90 depletion drove severe white adipose tissue (WAT) dysfunction, characterized by impaired lipogenic capacity, exacerbated lipolysis, and diminished local insulin signaling. This was accompanied by a pro-inflammatory secretory shift in WAT, evident from decreased Adipoq and increased Cd68/Ccl3 expression. In the liver, transcriptomic analysis revealed a profound induction of pathways related to fatty acid uptake and cytokine signaling. Mechanistically, ZFP90 forms a repressive complex with TRIM28, acting as a crucial molecular brake on NF-kB signaling. Loss of ZFP90 unleashes p65-mediated hyper-inflammation. Clinically, hepatic ZFP90 expression is significantly upregulated in patients with MASLD. ZFP90 is a novel regulator of immunometabolic homeostasis under dietary stress. By forming of complex with Trim28 to inhibit the nuclear translocation of NF-κB, ZFP90 suppresses pro-inflammatory responses and protects the liver from obesity-associated systemic lipotoxicity. These findings provide critical insights into the adipo-hepatic axis and highlight ZFP90 as a promising therapeutic target to mitigate the progression to metabolic dysfunction-associated steatohepatitis (MASH). - Source: PubMed
Publication date: 2026/07/16
Park SeongjoonKomatsu ToshimitsuMisumi KoheiOkuzaki DaisukeShimokawa Isao - Atopic dermatitis (AD) occurs across all ages but presents distinct clinical and immunologic features between children, adults, and older adults. The molecular programs underlying these age-specific immune differences remain poorly understood. - Source: PubMed
Publication date: 2026/06/01
Baldonado Gian Carlo LKumar SugandhJin JoyFang XiaohuiIldardashty AlexanderBraun MitchellNeuhaus Isaac MMathes ErinBhutani TinaLiao Wilson - Atopic dermatitis (AD) occurs across all ages but presents distinct clinical and immunologic features between children, adults, and older adults. The molecular programs underlying these age-specific immune differences remain poorly understood. - Source: PubMed
Publication date: 2025/11/25
Baldonado Gian Carlo LKumar SugandhJin JoyFang XiaohuiIldardashty AlexanderBraun MitchellNeuhaus Isaac MMathes ErinBhutani TinaLiao Wilson - Telomeric repeat binding factor 2 (TERF2), a key component of the Shelterin complex, is crucial for maintaining telomere integrity and genome stability. While the involvement of TERF2 in tumorigenesis and progression has been documented, comprehensive pan-cancer analyses of TERF2 across different malignancies remain scarce. - Source: PubMed
Publication date: 2025/02/24
Ma QiangXu WenGuo Xiaolan - Forkhead box protein P3 (FOXP3) is known to orchestrate the development and maintenance of T regulatory cells, a cell population specialized in immune suppression and peripheral immune tolerance. FOXP3 activity is fine-tuned through its interaction with several protein-binding partners. By using IntAct database, we retrieved three physical binary interactors: E3 ubiquitin-protein ligase CHIP, Zfp-90, and nuclear receptor ROR-α. Coevolution clusters between FOXP3 and its interactors were identified with the use of iBIS2 algorithm, the iterative version of BIS/BIS2. Most of the coevolving pairs came from some species of monotremes and marsupials, as well as from a group of bats, thus suggesting that protein interactions of FOXP3 with its partners may be changed and/or modulated during mammalian speciation. Furthermore, our analysis would suggest the occurrence of a determinant role of FOXP3 in suppressing pregnancy alloreactions in placental mammals. Similarly, FOXP3, through its interaction with different protein interaction mechanisms, would explain the unique control of inflammatory response to infections in bats. By identifying several inter-protein clusters between the different protein pairs, our findings may provide a guide for new therapeutic approaches to modulate T regulatory suppression and/or enhance immune tolerance. - Source: PubMed
Publication date: 2023/03/25
D'Amico FabioSkarmoutsou EvangeliaLibra Massimo