PDHX

Last update 08 May 2025

Basic Info

Synonyms

Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex, DLDBP, E3-binding protein

+ [8]

Introduction

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

100 Clinical Results associated with PDHX

100 Translational Medicine associated with PDHX

0 Patents (Medical) associated with PDHX

125

Literatures (Medical) associated with PDHX

01 Apr 2025·Poultry Science

Co-exposure to ammonia and lipopolysaccharide-induced impaired energy metabolism via the miR-1599/HK2 axis and triggered autophagy, ER stress, and apoptosis in chicken cardiomyocytes

Article

Author: Liu, Xiumei ; Qiu, Minna ; Tang, You ; Teng, Xiaohua ; Wang, Yan ; Liu, Yuhang ; Chang, Minghang ; Hao, Zhiyu ; Sun, Wei ; Liu, Yuhao

Ammonia (NH₃) and lipopolysaccharide (LPS), common pollutants in poultry farming environments, pose significant health risks by disrupting cellular processes. Although previous studies have demonstrated the individual effect of NH₃ or LPS on human and animal health, the mechanisms underlying their combined impact on chicken heart tissue remain poorly understood. In this study, we established a chicken cardiotoxicity model to investigate the effects of NH₃ and/or LPS exposure on energy metabolism, autophagy, endoplasmic reticulum (ER) stress, and apoptosis in cardiomyocytes. Our findings indicated that exposure to NH₃ or/and LPS reduced ATPase activity and ATP content, led to the downregulation of HK2, PK, PDHX, and SDH, and upregulation of AMPK, resulting in impaired energy metabolism in chicken cardiomyocytes. Additionally, we found the gga-miR-1599/HK2 axis as a key regulator involved in NH₃ or/and LPS-induced energy metabolism impairment. The impairment in energy metabolism activated the AMPK/mTOR pathway, which subsequently triggered autophagy, evidenced by the upregulation of Beclin, LC3-I, and LC3-II. Furthermore, decreased mTOR expression induced ER stress, as indicated by the upregulation of key markers such as ATF6, GRP78, IRE1, and PERK. ER stress, in turn, increased CHOP expression, which downregulated Bcl-2 and upregulated Bim, resulting in elevated levels of Bax, caspase-9, and caspase-3, ultimately triggering apoptosis. This study provides valuable insights into the mechanisms of NH₃ and LPS co-exposure on poultry heart tissue and identifies potential molecular targets for mitigating these adverse effects.

01 Feb 2025·Developmental & Comparative Immunology

Oridonin inhibits SGIV infection by regulating glycolipid metabolism and inflammatory response

Article

Author: Qin, Qiwei ; Wei, Shina ; Jiang, Yunxiang ; Chen, Jiatao ; Ruan, Leshan

Singapore grouper iridovirus (SGIV) is a significant infectious disease in the grouper aquaculture industry. Currently, there is no effective drug available to prevent or treat SGIV. Oridonin (Ori) is a naturally occurring compound derived from Rabdosia rubescens, exhibiting various biological activities, including anti-tumor, anti-inflammatory, and antioxidant properties. In this study, we examined the anti-SGIV activity of Ori and its potential mechanism of action in vitro. The study results indicate that Ori effectively inhibits SGIV infection at various concentrations. Further studies reveal that Ori inhibits the formation of lipid droplets induced by SGIV infection. Additionally, Ori suppresses the SGIV-induced up-regulation of fatty acid synthesis-related genes (SREBP1, ACC1, SCD1, FASN) and glycolysis-related genes (GLUT1, GLUT2, HK2, PDHX). The mTOR pathway plays a crucial role in regulating glycolipid metabolism. Our findings indicate that Ori suppresses the phosphorylation of AKT and mTOR proteins. Further research revealed that the activation or inhibition of mTOR significantly impacts SGIV protein production and the expression of genes related to glycolipid metabolism. In addition, Ori effectively inhibits the up-regulation of NLRP3, ASC, Caspase-1, and pro-inflammatory cytokines induced by SGIV infection. In conclusion, our experimental findings indicate that Ori effectively inhibits SGIV infection by regulating glycolipid metabolism through the AKT/mTOR pathway and by suppressing the inflammatory responses triggered by SGIV infection.

04 Jan 2025·Protein & Cell

PDHX acetylation facilitates tumor progression by disrupting PDC assembly and activating lactylation-mediated gene expression

Article

Author: Mao, Qiankun ; Jiang, Zetan ; Gao, Ping ; Liu, Haiying ; Xiong, Nanchi ; Shen, Shengqi ; Ye, Ling ; Li, Shi-ting ; Yan, Ronghui ; Zhang, Huafeng ; Jia, Weidong ; Sun, Yuchen ; Zhang, Pinggen

AbstractDeactivation of the mitochondrial pyruvate dehydrogenase complex (PDC) is important for the metabolic switching of cancer cell from oxidative phosphorylation to aerobic glycolysis. Studies examining PDC activity regulation have mainly focused on the phosphorylation of pyruvate dehydrogenase (E1), leaving other post-translational modifications largely unexplored. Here, we demonstrate that the acetylation of Lys 488 of pyruvate dehydrogenase complex component X (PDHX) commonly occurs in hepatocellular carcinoma, disrupting PDC assembly and contributing to lactate-driven epigenetic control of gene expression. PDHX, an E3-binding protein in the PDC, is acetylated by the p300 at Lys 488, impeding the interaction between PDHX and dihydrolipoyl transacetylase (E2), thereby disrupting PDC assembly to inhibit its activation. PDC disruption results in the conversion of most glucose to lactate, contributing to the aerobic glycolysis and H3K56 lactylation-mediated gene expression, facilitating tumor progression. These findings highlight a previously unrecognized role of PDHX acetylation in regulating PDC assembly and activity, linking PDHX Lys 488 acetylation and histone lactylation during hepatocellular carcinoma progression and providing a potential biomarker and therapeutic target for further development.

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