Ask about this productRelated genes to: HDAC2 Blocking Peptide
- Gene:
- HDAC2 NIH gene
- Name:
- histone deacetylase 2
- Previous symbol:
- -
- Synonyms:
- RPD3, YAF1, KDAC2
- Chromosome:
- 6q21
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-15
- Date modifiied:
- 2019-02-19
Related products to: HDAC2 Blocking Peptide
Related articles to: HDAC2 Blocking Peptide
- The interaction between Astragaloside IV (AS-IV) and the gut microbiota is known to help prevent cardiovascular disease, however, its underlying mechanism through which AS-IV modulates the balance of intestinal flora to ameliorate heart failure (HF) remains unclear. - Source: PubMed
Publication date: 2026/09/16
Shi MinWei JiamingYuan HuiGuo Zhihua - Melanoma therapies can produce substantial tumor regression without durable control, raising two separable questions: how efficiently tumor cells are eliminated and whether therapy-induced death supports immune recognition. This review examines whether melanocytic-lineage redox biology and site-selective protein S-nitrosylation help connect these outcomes. We distinguish mechanisms demonstrated directly in melanoma from mechanistic precedents in other systems and from hypotheses that require validation. In melanocytic cells, active pigment-forming chemistry can support a nitric oxide synthase (NOS)-active state. In melanoma, S-nitrosylation has been linked to MAPK persistence during MEK inhibition, TSC2-dependent mTOR activation, and NOS1-dependent suppression of interferon programs through HDAC2 and IRF7. Pharmacological S-nitrosylation blockade also increases ER stress signaling, calreticulin exposure, HMGB1 release, immune cell recruitment, and tumor control, but these observations do not establish a site-specific effect on the immunological quality of cell death. We therefore propose a two-gate framework in which S-nitrosylation may regulate both susceptibility to irreversible death and the signaling competence of dying cells. Establishing this model will require quantitative site occupancy, cell type-resolved nitrosoproteomics, causal site replacement, and immune assays that distinguish altered signaling from simply increased cell killing. The available evidence supports selective interrogation of causal S-nitrosylation nodes rather than indiscriminate suppression of NO biology. - Source: PubMed
Publication date: 2026/09/14
Srivastava JyotiPremi Sanjay - Per- and polyfluoroalkyl substances (PFAS) are omnipresent, persistent contaminants associated with rising ovarian cancer incidence; however, the molecular circuitry linking PFAS to ovarian tumorigenesis remains obscure. - Source: PubMed
Publication date: 2026/08/28
Wang YuluLiu XueliDing YananZhao ZhanjieChen HaotianWu XiaojuanYang YanzhouPan PenggeLi LuyiGao Hui - Tumor maturation is a property of neuroblastomas but can also be observed in unique cases of primary brain malignancies. We hypothesized that the mechanisms of peripheral and central neurogenic tumor maturation could be similar. This study encompassed 19 cases of neuroblastoma and solitary cases of CNS tumors having undergone a morphologically verified maturation. The tumors were analyzed by sequencing and gene expression profiling. We revealed potential similarity of different tumor types upon maturation, associated with stimulated MAPK, PI3K-AKT-mTOR, and TrkA signaling and suppressed regulation of cell cycle and DNA replication and repair. Tumors completing maturation similarly showed enhanced immunogenicity. The levels of NTRK2 expression increased during maturation. Expression of NTRK1 and positive epigenetic regulators (SWI/SNF subunits) increased prior to maturation and decreased upon the differentiation completion. Expression of negative epigenetic regulators EZH2, HDAC10, HDAC2, and DNMT3A decreased in maturing tumors. These data suggest that central and peripheral neurogenic tumors are likely to have common maturation mechanisms. Molecular scenarios associated with neuroblastoma maturation could be: (1) TrkA signaling (seen in cases presenting in < 18-month-olds), or (2) altered expression of epigenetic regulators and transcription factors (seen in cases presenting in >18-month-olds); treatment-induced maturation of CNS malignancies could involve both scenarios. - Source: PubMed
Publication date: 2026/09/11
Druy Alexander EZverev Ivan AAndreeva Natalia ATarakanova Alexandra VSenchenko Maria AGegeliya Nina VZaytseva Margarita ASanakoeva Agunda VPanferova Agnesa VAbasov Ruslan KUsman Natalia YPetrova Vera SKonovalov Dmitry MRaskin Grigorii ANovichkova Galina AGrachev Nikolay SShamanskaya Tatyana VKachanov Denis YPapusha Ludmila I - Psoriasis is a chronic and recurrent inflammatory dermatosis characterized by dysregulated keratinocyte proliferation. Calcium-binding protein 39 (CAB39), a critical regulatory scaffold for Sterile 20 kinase, has been implicated in multiple diseases, but its role and regulatory mechanisms in psoriasis remain unclear. Here, we found that CAB39 was significantly upregulated in psoriatic lesions, and CAB39 knockdown inhibited keratinocyte proliferation and attenuated psoriasis progression. Further investigations revealed that CAB39 crotonylation at lysine 196 was reduced in psoriatic lesions. Functional analyses in normal human epidermal keratinocytes (NHEKs) showed that the crotonylation-deficient CAB39 K196A mutant significantly promoted keratinocyte hyperproliferation and glycolytic remodeling. Dysregulation of modifying enzymes, including downregulated CBP and upregulated HDAC2/3, drives CAB39 K196 decrotonylation in psoriasis. Mechanistically, CAB39 K196 decrotonylation weakens its binding affinity to STRAD (STE20-related adaptor), disrupts the stability of the CAB39-STRAD-LKB1 (liver kinase B1) complex, and inhibits the LKB1/AMPK signaling pathway. Concurrently, decrotonylated CAB39 promotes phosphatidic acid (PA, a lipid second messenger) synthesis, activating the pro-proliferative PA/MAPK/mTOR signaling cascade. Our findings uncover a novel pathogenic mechanism in psoriasis, wherein CAB39 K196 decrotonylation drives keratinocyte dysfunction, and expand our understanding of non-histone crotonylation in inflammatory skin diseases. Importantly, targeting the CBP/HDAC2/3-CAB39 crotonylation axis may represent a potential therapeutic strategy for psoriasis. - Source: PubMed
Liang HuifangLi JunqinJing WeixiaZhang Kaiming