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Last update 08 May 2025

ABHD10

Last update 08 May 2025

Basic Info

Synonyms

ABHD10, abhydrolase domain containing 10, depalmitoylase, Abhydrolase domain-containing protein 10

+ [5]

Introduction

Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins (PubMed:31740833). Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability (PubMed:31740833). Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate (PubMed:22294686).

Drugs associated with ABHD10

ML257

Target

ABHD10

Mechanism

ABHD10 inhibitors

Active Org.-

Originator Org.

The Scripps Research Institute

Active Indication-

Inactive Indication

Malignant glioma of brain

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ABHD10

100 Translational Medicine associated with ABHD10

0 Patents (Medical) associated with ABHD10

Literatures (Medical) associated with ABHD10

01 Dec 2024·International Immunopharmacology

Use of mendelian randomization to assess the causal associations of circulating plasma proteins with 12-lead ECG parameters

Article

Author: Yu, Zhongzhi ; Liu, Xinxin ; Zhao, Peng ; Wang, Yan ; Han, Feiyuan ; Meng, Li ; Yu, Bo ; Wang, Yidan ; Wu, Yunfei ; Tian, Jinwei

BACKGROUNDCardiac conduction disorders predispose individuals to arrhythmias, currently but the exact mechanisms of cardiac conduction remain elusive. The study sought to identify the causal association between circulating plasma proteins and electrocardiogram (ECG) traits, offer valuable biological insights and clinical guidance into cardiac conduction.METHODSProteome-wide Mendelian randomization (MR) analysis was firstly conducted to assess causal associations between plasma proteins and five ECG traits, including P wave duration (PWD), QRS duration, PR, QT and RR intervals. Multiple sensitivity analyses were implemented. The reverse MR analysis, colocalization analysis and replication analysis were used to consolidate the reliability of our results. Then, we conducted mediation analysis to explore potential mechanism between plasma proteins and ECG traits. The gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses were applied to clarify the biological functions of target proteins. Finally, phenome-wide MR (Phe-MR) and drug databases were searched.RESULTSWe identified 3 proteins (FAM151A, VEGF165, VEGF121) associated with PWD, 12 proteins (ABHD10, ADK, Cathepsin_S, DUSP13, Ephrin_A3, MAPRE2, OMG, PAM, PMM1, SH3BGRL3, TCP4, SYT11) linked to PR interval, 1 protein (PKC_A) related to QRS duration, and 2 proteins (MXRA7, SVEP1) associated with QT interval. A significant causal effects of ECG traits on them was not found in reverse MR. Colocalization and replication analyses strengthened our findings further. The impacts were partly mediated by anthropometric measures. Enrichment analysis of target proteins mainly enriched for multiple key pathways such as regulation of hydrolase activity and fibronectin binding. Through drug databases searching, 5 identified proteins (VEGFA, ADK, PAM, Cathepsin_S, PKC_A) were considered druggable.CONCLUSIONSWe discovered significant causal associations between genetically predicted levels of 18 plasma proteins and ECG traits. These results highlight the importance of circulating plasma proteins in cardiac conduction and open up the possibility of novel arrhythmia drug development.

03 Jul 2023·Communications biology

The Elk-3 target Abhd10 ameliorates hepatotoxic injury and fibrosis in alcoholic liver disease.

Article

Author: Zhang, Cong-Ying ; Zhou, Jing ; Wang, Wen-Tao ; Shi, Tie-Wei ; Bai, Chun-Ying ; Li, Tian-Zhu ; Wu, Bao

Alcoholic liver disease (ALD) and other forms of chronic hepatotoxic injury can lead to transforming growth factor β1 (TGFβ1)-induced hepatic fibrosis and compromised liver function, underscoring the need to develop novel treatments for these conditions. Herein, our analyses of liver tissue samples from severe alcoholic hepatitis (SAH) patients and two murine models of ALD reveals that the ALD phenotype was associated with upregulation of the transcription factor ETS domain-containing protein (ELK-3) and ELK-3 signaling activity coupled with downregulation of α/β hydrolase domain containing 10 (ABHD10) and upregulation of deactivating S-palmitoylation of the antioxidant protein Peroxiredoxin 5 (PRDX5). In vitro, we further demonstrate that ELK-3 can directly bind to the ABHD10 promoter to inhibit its transactivation. TGFβ1 and epidermal growth factor (EGF) signaling induce ABHD10 downregulation and PRDX5 S-palmitoylation via ELK-3. This ELK-3-mediated ABHD10 downregulation drives oxidative stress and disrupts mature hepatocyte function via enhancing S-palmitoylation of PRDX5's Cys100 residue. In vivo, ectopic Abhd10 overexpression ameliorates liver damage in ALD model mice. Overall, these data suggest that the therapeutic targeting of the ABHD10-PRDX5 axis may represent a viable approach to treating ALD and other forms of hepatotoxicity.

01 Dec 2019·Nature Chemical Biology

ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5

Article

Author: Qiu, Tian ; Kathayat, Rahul S ; Dickinson, Bryan C ; Fukata, Masaki ; Thorne, Anneke K ; Cao, Yang ; Fukata, Yuko ; Azizi, Saara-Anne ; Rice, Phoebe A ; Ahn, Daniel

S-Palmitoylation is a reversible lipid post-translational modification that has been observed on mitochondrial proteins, but both the regulation and functional consequences of mitochondrial S-palmitoylation are poorly understood. Here, we show that perturbing the 'erasers' of S-palmitoylation, acyl protein thioesterases (APTs), with either pan-active inhibitors or a mitochondrial-targeted APT inhibitor, diminishes the antioxidant buffering capacity of mitochondria. Surprisingly, this effect was not mediated by the only known mitochondrial APT, but rather by a resident mitochondrial protein with no known endogenous function, ABHD10. We show that ABHD10 is a member of the APT family of regulatory proteins and identify peroxiredoxin-5 (PRDX5), a key antioxidant protein, as a target of ABHD10 S-depalmitoylase activity. We then find that ABHD10 regulates the S-palmitoylation status of the nucleophilic active site residue of PRDX5, providing a direct mechanistic connection between ABHD10-mediated S-depalmitoylation of PRDX5 and its antioxidant capacity.

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ABHD10

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