HDAC4, GST, Human Protein
- Known as:
- HDAC4, GST, Human Protein
- Catalog number:
- z03045-50
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Genscript
- Gene target:
- HDAC4 GST Human Protein
Related genes to: HDAC4, GST, Human Protein
- Gene:
- HDAC4 NIH gene
- Name:
- histone deacetylase 4
- Previous symbol:
- BDMR
- Synonyms:
- KIAA0288, HDAC-A, HDACA, HD4, HA6116, HDAC-4
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-11-28
- Date modifiied:
- 2015-09-11
Related products to: HDAC4, GST, Human Protein
Related articles to: HDAC4, GST, Human Protein
- Histone lactylation links lactate metabolism to chromatin regulation, but whether lactylation-program-associated transcriptional patterns delineate recurrent pan-cancer tumor states remains unclear. - Source: PubMed
Publication date: 2026/07/31
Bo ZhihaoZhang ShiyueZheng ZhiyuanMa JialuFeng YuankangLi JianqiaoLiu YangFu ZhinanXing HaotianYu ShuminGuo ShaominSi XianjingWang JiahaoWang RunpengWang RuiZhang XilingYue DanWang Yong - Arteriovenous fistula (AVF) maturation is characterized by outward remodeling presented mainly as wall thickening and lumen enlargement, probably mediated by increased differentiated vascular smooth muscle cells (VSMCs) and extracellular matrix (ECM) deposits, at least in part. Our previous study revealed that the highly conserved transcription factor early growth response protein 2 (EGR2) promoted renal tubular epithelial cell differentiation and ECM accumulation. Here, we found that EGR2 expression was enhanced in venous outflow tracts from end-stage renal disease (ESRD) patients and mice with AVF surgery accompanied by a thickened venous wall and enlarged lumen. Then, the knockdown of EGR2 could inhibit AVF maturation while EGR2 overexpression further promoted outward remodeling in AVF mice with adeno-associated virus (AAV) administration regulated by differentiated VSMCs and ECM deposition. Mechanistically, gene deletion of EGR2 inhibited c-Myc possibly by binding to the promoter region of the insulin-like growth factor 2 binding protein 2 (IGF2BP2) gene. Moreover, EGR2 was upregulated by histone deacetylase 4 (HDAC4) which probably negatively regulated transcription factor c-Jun, the latter was reported to antagonize the effect of EGR2. Thus, we speculated that EGR2 is upregulated by HDAC4 possibly by negatively regulating c-Jun and promoting outward remodeling through the IGF2BP2/ c-Myc signaling axis during AVF maturation. - Source: PubMed
Publication date: 2026/07/29
Song AnniYan RuiweiHuang MingyuZou XingjianGao PanCai ChuanqiYin XingjieLuo PengliZhu PingZhang Chun - Inspired by reports that HDAC blockade can trigger compensatory activation of the LIFR-JAK1-STAT3 axis in solid tumors, we designed and synthesized a series of niclosamide-based STAT3/HDAC dual-target inhibitor candidates by incorporating a SAHA-derived hydroxamate zinc-binding group into the pleiotropic, STAT3-modulating niclosamide scaffold. Biological evaluation identified NS06 as the best-balanced analogue, with IC values of 1.49 and 1.41 μM against MDA-MB-231 and HCT116 cells, respectively. Mechanistic studies showed that NS06 bound STAT3 in vitro (SPR, K = 5.82 μM), suppressed STAT3 phosphorylation, and inhibited HDAC1, HDAC3, and HDAC6 with IC values of 129.1, 451.2, and 230.4 nM, respectively, while showing limited inhibition of HDAC4 and HDAC11 in the primary screen. NS06 also increased histone H3 acetylation, induced apoptosis, and inhibited migration and colony formation. In addition, NS06 retained antiproliferative activity in a 3D tumor spheroid model and showed improved Caco-2 permeability together with moderate liver microsomal stability (t ≈ 48.6 min in rat liver microsomes). Docking and 100-ns molecular dynamics simulations further supported chemically plausible binding modes in the HDAC1 catalytic pocket and the STAT3 SH2 domain. Overall, these findings support niclosamide as a tractable scaffold for mechanism-driven STAT3/HDAC dual-target inhibitor design and identify NS06 as a promising lead for further optimization against solid tumors. - Source: PubMed
Publication date: 2026/07/25
Shi YuchenZhang QihaoWang ChenxiLu ZipengChen FangfangHan LiuXu ZhouyangZhang YuanMa ShumeiYe FaqingWang Xuebao - Skeletal muscle is crucial for glucose regulation and amino acid storage, significantly influencing overall metabolic balance. Its function is tightly regulated by complex mechanisms, with histone acetylation as a key epigenetic control point. Our previous work identified eIF6 as a key regulator of muscle energy homeostasis and demonstrated its role in modulating histone acetylation in the liver. However, whether similar epigenetic mechanisms underpin eIF6's effects in muscle remains undetermined. To investigate this, we measured H3K9 acetylation levels and HDAC activity both in vivo, using eIF6 mice, and in vitro, following eIF6 depletion. Our findings demonstrate that eIF6 downregulation in C2C12 myoblasts drives an increase in histone acetylation, a pattern also evident in heterozygous eIF6 primary satellite cells, both in their undifferentiated state and following differentiation. In vivo, eIF6 mice show pronounced histone hyperacetylation, especially in younger animals, which correlates with a specific decrease in class II HDACs, particularly HDAC4 and HDAC5. This trend is further supported by in vitro data and findings from Drosophila eIF6 mutants, both of which exhibit decreased HDAC activity. Importantly, the reduction in HDAC4 and HDAC5 activity appears to result from decreased protein levels, driven by eIF6-dependent translational regulation of their mRNAs. All together, these findings establish a link between mRNA translation and histone acetylation in muscle, underpinning translational control as a master regulator of histone acetylation. - Source: PubMed
Publication date: 2026/07/29
Scagliola AlessandraMiluzio AnnaritaFerrari IvanBrina DanielRicciardi SaraBiffo Stefano - The hypoxia-inducible factor (HIF) signaling pathway is essential for cellular adaptation to low oxygen. Although the canonical PHD-pVHL pathway that mediates HIF-α degradation under normoxia is well established, alternative regulatory mechanisms remain poorly understood. Here, we identify Microrchidia family CW-type zinc-finger 2 (MORC2) as a negative regulator of HIF-α. In zebrafish, CRISPR/Cas9-generated mutants developed polycythemia, systemic hypoxia, and constitutive activation of the HIF pathway. Mechanistically, MORC2 counteracts histone deacetylase 4 (HDAC4) by competing for HIF-1α binding. Loss of MORC2 enhances HDAC4 recruitment to HIF-1α, reducing acetylation at lysine 629 and preventing proteasomal degradation of HIF-1α. These results define a regulatory mechanism in which MORC2 modulates HIF-1α stability via HDAC4 mediated deacetylation, shedding light on hematopoiesis and HIF-related disorders. - Source: PubMed
Publication date: 2026/07/27
Tang YanfeiZhang BoqiXue TingtingLiu YunzhangLi YunGu YuchaoHao JiejieLu Ling