HDAC6
- Known as:
- HDAC6
- Catalog number:
- 000427A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- HDAC6
Related genes to: HDAC6
- Gene:
- HDAC6 NIH gene
- Name:
- histone deacetylase 6
- Previous symbol:
- -
- Synonyms:
- KIAA0901, JM21, HD6, FLJ16239, PPP1R90
- Chromosome:
- Xp11.23
- Locus Type:
- gene with protein product
- Date approved:
- 2000-11-28
- Date modifiied:
- 2015-09-11
Related products to: HDAC6
Related articles to: HDAC6
- Spinal muscular atrophy (SMA) is a severe neuromuscular disorder caused by SMN gene defects. It leads to motor neuron death and muscle weakness. Without treatment, most affected children don't survive past age two. Recently, new gene therapies help SMA children survive, but treated patients now face ongoing muscle atrophy and functional deficits, creating a novel clinical presentation. Over the last years, treatments of various animal models of neuromuscular disorders have shown the ability of inhibitors of the non-conventional histone deacetylase 6 (HDAC6) to reduce muscle atrophy. This study examines HDAC6 inhibition's impact on muscle cell differentiation and tests in vivo if combining it with new standard SMA treatments improves muscle and overall condition in SMA mice. Here, we report that HDAC6 controls myotube formation and maturation in vitro. In particular, HDAC6 inhibition increases the size of SMA patients-derived muscle primary myotubes. In vivo, when combined with ASOs inducing exon-7 inclusion in SMN2 RNA, HDAC6 systemic inhibition strongly improved muscle strength, mass, function, and longevity of SMA-like mice model. These findings provide evidence that selective inhibition of HDAC6 improves myogenic progression. Hence, HDAC6 inhibitors are good candidates to ameliorate persisting symptoms of SMA patients treated with the new standard of care. - Source: PubMed
Publication date: 2026/05/02
Osseni AlexisSlika RashaCoudert LaurentConjard-Duplany AgnèsWeill LaureBelotti EdwigeSiopi EleniGangloff Yann-GaëlSapaly DelphineBendris SabrinaClerc ZoéBruneteau GaëlleVuillerot CaroleLeblanc PascalCharbonnier FrédéricSchaeffer Laurent - Gingival squamous cell carcinoma (GSCC) is a rare subset of oral squamous cell carcinoma (OSCC), often mimicking benign or inflammatory lesions, which complicates early diagnosis. Chronic inflammation plays a pivotal role in oral carcinogenesis, yet its molecular implications in GSCC remain underexplored. This Prognostic Systematic Literature Review (SLR) presents a case-based review of GSCC and evaluates the immunohistochemical expression of key inflammatory markers - COX-2, TNF-α, IL-6, NF-κB, VEGF, iNOS, Bcl-2/Bax ratio, and HDAC6 - in OSCC to assess their diagnostic, prognostic, and therapeutic relevance. Literature search was done (1999-2025) across PubMed, Scopus, Web of Science, Cochrane, and Google Scholar to identify studies on biomarker analysis in histopathologically confirmed cases of OSCC. Data extraction focused on clinical presentation, tumour grade, invasion, metastasis, and survival. Study quality was assessed using NOS and JBI tools. From 1055 screened records,18 studies met inclusion criteria. GSCC is often masqueraded as desquamative gingivitis or periodontal abscess, causing diagnostic delays. Immunohistochemistry revealed frequent overexpression of COX-2, TNF-α, VEGF, and Bcl-2, correlating with tumour aggressiveness, angiogenesis, higher histological grade, and poor prognosis. Temporal trends indicate a shift from apoptotic dysregulation to cytokine-driven inflammatory phenotypes as key drivers of OSCC progression. To Conclude, GSCC requires high clinical vigilance due to its deceptive presentation. Biomarkers such as COX-2, TNF-α, IL-6, NF-κB, and VEGF provide critical prognostic and therapeutic insights, emphasising the role of inflammation in tumour progression and supporting biomarker-guided early detection strategies. - Source: PubMed
Publication date: 2026/04/02
Hussain Sajid TManipal SunayanaJeddy NadeemRadhika TMohideen Khadijah - Histone deacetylase 6 (HDAC6) is a unique, predominantly cytoplasmic enzyme that regulates a broad spectrum of cellular and physiological processes, including cell proliferation, migration, intracellular transport, and differentiation. Its distinct structural configuration, comprising two catalytic deacetylase domains and a zinc finger ubiquitin-binding domain (ZnF-BUZ), enables HDAC6 to deacetylate a variety of non-histone substrates, such as α-tubulin, heat shock protein 90 (Hsp90), cortactin, and peroxiredoxin (Prdx). Furthermore, HDAC6 plays a key role in cellular stress responses and cell survival by facilitating the clearance of misfolded proteins, inducing autophagy, and modulating the unfolded protein response. Despite its cytoprotective roles, HDAC6 has emerged as a therapeutic target due to its involvement in multiple pathological pathways and age-related disorders. Tubastatin A (Tub A), a novel and highly selective HDAC6 inhibitor, demonstrates strong therapeutic potential against neurodegenerative, cardiovascular, autoimmune, metabolic, cancer, and other diseases. Tub A enhances the acetylation of both histone and non-histone proteins, thereby modulating gene expression and diverse cellular processes. It shows pharmacological effects, including anti-inflammatory, neuroprotective, anti-diabetic, anti-obesity, anti-oxidant, and other activities. Moreover, preclinical evidence suggests that Tub A effectively regulates multiple pathological pathways by inhibiting HDAC6, which contributes to ameliorating age-related disorders. Therefore, Tub A represents a promising epigenetic modulator with broad therapeutic relevance. Hence, further comprehensive and large-scale investigations are warranted to elucidate its clinical potential and its roles in disease management, as no clinical data related to Tub A activity are available. This review highlights the therapeutic potential of the selective HDAC6 inhibitor Tub A across various pathological conditions, discusses current preclinical findings, and outlines key challenges and future directions for clinical translation. - Source: PubMed
Publication date: 2026/04/17
Rajput SonuSingh Sumeet KumarYadav PoonamKhurana AmitWeiskirchen RalfNavik Umashanker - Histone deacetylase inhibitors (HDACis) are a class of epigenetic drugs that, as the name suggests, inhibit histone deacetylases (HDACs), which are anticancer therapeutic targets. Several studies have investigated hydroxamic acid HDACi. However, most anti-cancer HDACis are pan-inhibitors with multiple adverse reactions. Compared with traditional anti-tumor drugs, natural products have lower toxicity and are less likely to cause drug resistance in tumor cells. Our previous study identified that chalcone natural products have strong anti-tumor activity in vitro. Therefore, in this study, 27 chalcone derivatives with α, β-unsaturated hydroxamic acid groups were synthesized and evaluated in vitro and in vivo. The results showed that compound 4u had a strong inhibitory effect on SW620 cell proliferation. Furthermore, 4u selectively inhibits HDAC6 activity, as validated by the strong binding affinity observed between 4u and HDAC6. Furthermore, in vitro results were validated by in vivo assays, showing that 4u could inhibit tumor growth and HDAC6 activity in an animal model. These findings confirmed that compound 4u can serve as a lead compound for selective HDAC6 inhibitors and warrant further research as an anti-tumor agent. - Source: PubMed
Publication date: 2026/04/24
Ma XinLi SiqiHuang XinyueMa MengyanDeng BoyanWang YanlingWen Ran - Histone deacetylases (HDACs) regulate transcription by removing acetyl groups from lysines, and their dysregulation promotes cancer. Clinically approved HDAC inhibitors show limited isoform selectivity, toxicity, and modest efficacy in solid tumors. We therefore designed and synthesized uracil-based hydroxamic acids (UBHAs) bearing systematic cap group and linker modifications. Several compounds achieved nanomolar inhibition, particularly against HDAC6, and reduced activity toward class I isoforms. Structure-activity relationships highlight that -substituted phenyl moieties and four-carbon linkers enhance potency. Compounds and emerged as lead candidates, reducing cancer cell viability at submicromolar doses while sparing noncancerous cells. In U937 cells, both promoted cell-cycle arrest, apoptosis, and H3K9 and α-tubulin acetylation, alongside modulation of apoptosis-related genes and microRNAs. In prostate cancer models, inhibited AR and AR cell proliferation, enhanced histone and tubulin acetylation, upregulated p21, and downregulated Bcl-2. These findings identify biphenyl-substituted UBHAs as promising therapeutics and probes to dissect HDAC biology. - Source: PubMed
Publication date: 2026/04/30
Fiorentino FrancescoBontempi GiulioMichetti FedericaPecci ValeriaFabbrizi EmanuelePasseri DanielaCorsetti LetiziaFarini ValentinaCasano FabrizioGioiello AntimoDi Sotto AntonellaPellicciari RobertoBufalo Donatella DelTrisciuoglio DanielaNanni SimonaStrippoli RaffaeleMai AntonelloRotili Dante