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Last update 08 May 2025

HDAC10

Last update 08 May 2025

Basic Info

Synonyms

DKFZP761B039, HD10, HDAC10

+ [2]

Introduction

Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Histone deacetylase activity has been observed in vitro (PubMed:11677242, PubMed:11726666, PubMed:11739383, PubMed:11861901). Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039). The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:28516954). May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:23801752, PubMed:29968769). May play a role in homologous recombination (PubMed:21247901). May promote DNA mismatch repair (PubMed:26221039).

Drugs associated with HDAC10

5e(TES Pharma)

Target

HDAC1 x HDAC10 x HDAC2 x HDAC3 x HDAC6 x HDAC8

Mechanism

HDAC1 modulators [+5]

Active Org.

Fudan University

Originator Org.

TES Pharma SRL

Active Indication

Ovarian Epithelial Carcinoma

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

FM60

Target

HDAC10

Mechanism

HDAC10 inhibitors

Active Org.

Georgetown Lombardi Comprehensive Cancer Center

Originator Org.

Georgetown Lombardi Comprehensive Cancer Center

Active Indication

Melanoma

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

TH-34

Target

HDAC10 x HDAC6 x HDAC8

Mechanism

HDAC10 inhibitors [+2]

Active Org.-

Originator Org.-

Active Indication-

Inactive Indication

Neuroblastoma

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with HDAC10

100 Translational Medicine associated with HDAC10

0 Patents (Medical) associated with HDAC10

195

Literatures (Medical) associated with HDAC10

01 Dec 2025·Molecular Biology Reports

A pilot study on the efficacy of a telomerase activator in regulating the proliferation of A375 skin cancer cell line

Article

Author: Pathak, Surajit ; Paul, Sujay ; Makalakshmi, M K ; Sharma, Neeta Raj ; Banerjee, Antara ; Anandan, B

INTRODUCTIONThe changes in histone modifications are linked to the progression of benign and normal tissue to malignancy. Thus, numerous findings suggest that targeting epigenetic factors might be a focus for anti-cancer treatment. In this study, we tested the hypothesis that telomerase activator might be a potential epigenetic regulator in combatting skin cancer cell proliferation.METHODSMelanoma cell line A375 cells were treated with telomerase activator TA-65. Cell senescence assay was done to evaluate the senescence induction. Morphological changes and differences in expression of HDACs and hTERT genes were studied. Further, hyaluronidase and anti-oxidant assays were also performed. Additionally, telomerase enzyme and 20S proteasome activity was also studied.RESULTSMorphological changes were observed in treated cells and it is evident that telomerase activator induced cellular senescence in high concentrations. From our results, it is evident that HDAC8 and HDAC10 expression was upregulated, whereas hTERT gene expression was downregulated in treated groups. This suggests that the telomerase activator has a regulatory role in skin cancer cells proliferation by targeting the epigenetic factors.CONCLUSIONTargeting HDACs and hTERT in the treatment of melanoma is a prominent concern. In our current study, we highlight the most recent research, although in its initial stage, involving various epigenetic factors involved in melanoma cells proliferation.

14 Feb 2025·ACS Pharmacology & Translational Science

Spirotetrahydroisoquinoline-Based Histone Deacetylase Inhibitors as New Antifibrotic Agents: Biological Evaluation in Human Fibroblasts from Bronchoalveolar Lavages of Idiopathic Pulmonary Fibrosis Patients

Article

Author: Altucci, Lucia ; Vincenzi, Fabrizio ; Pistocchi, Anna ; Saponara, Simona ; Bargagli, Elena ; Bergantini, Laura ; Papulino, Chiara ; Carbone, Sabrina ; Scalvini, Laura ; Gangi, Sara ; Fontana, Anna ; Varani, Katia ; Mor, Marco ; Contri, Chiara ; Campiani, Giuseppe ; Benedetti, Rosaria ; Cameli, Paolo ; Lodola, Alessio ; Pezzotta, Alex ; Pasquini, Silvia ; Carullo, Gabriele ; Butini, Stefania ; D’Alessandro, Miriana ; Gemma, Sandra

Idiopathic pulmonary fibrosis (IPF) is a rare interstitial lung disease typified by a progressive fibrosing phenotype. IPF has been associated with aberrant HDAC activity, particularly HDAC6. Combining synthetic and modeling studies, a new family of spirotetrahydroisoquinoline-capped histone deacetylase inhibitors 5a-o was developed. These analogues were prepared via the three-component Castagnoli-Cushman reaction (CCR) as the key step. Structure-activity relationship (SAR) studies identified 5n (fibrostat) as a preferential HDAC6 inhibitor with a suitable degree of selectivity compared to HDAC1, HDAC3, HDAC5, HDAC8, HDAC10, and HDAC11. 5n was able to negatively modulate the expression of fibrotic markers, fibronectin and collagen 1, in fibroblasts derived from bronchoalveolar lavages of IPF patients. In another ex vivo IPF human model, 5n (fibrostat) reduced the expression of fibronectin and negatively affected the expression of collagen 1 and vimentin, the latter being associated with invasiveness. Finally, fibrostat did not show toxicity in rat-perfused heart and zebrafish larvae.

01 Feb 2025·Poultry Science

High levels of histone acetylation modifications promote the formation of PGCs

Article

Author: Geng, Qingqing ; Cheng, Fufu ; Zuo, Qisheng ; Zhao, Ziduo ; Zhang, Yani ; Wu, Yuhui ; Niu, Yingjie ; Wang, Zhe

This study investigates the role of histone acetylation in the differentiation of chicken embryonic stem cells (ESCs) into primordial germ cells (PGCs). Transcriptomic sequencing was used to analyze differentially expressed genes during this differentiation process, with functional annotation identifying genes associated with histone acetylation. To explore the role of acetylation, acetate and an acetyltransferase inhibitor (ANAC) were added to the ESCs induction medium. Transcriptomic analysis revealed that during ESCs differentiation into PGCs, genes involved in histone acetyltransferase activity were upregulated, while those associated with histone deacetylase activity were downregulated. Functional enrichment analysis indicated these genes are involved in pathways critical for germ cell differentiation, underscoring their importance in avian reproductive biology. Quantitative real-time PCR (qRT-PCR) confirmed significant differential expression of HAT8 and HDAC10 between ESCs and PGCs (P < 0.01). The acetate treatment group exhibited a significantly higher number of embryoid bodies and elevated expression levels of CVH, C-KIT, and NANOS3 compared to the ANAC group (P < 0.01). Furthermore, indirect immunofluorescence and flow cytometry demonstrated a significantly higher proportion of DDX4-positive cells in the acetate group (P < 0.01). These findings provide preliminary evidence that histone acetylation regulates chicken PGCs formation, offering a theoretical framework for the epigenetic induction of PGCs in vitro. This study enhances our understanding of the molecular mechanisms underlying PGCs development in poultry and contributes to advancements in avian reproductive technologies and genetic conservation.

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HDAC10

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