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Last update 08 May 2025

TXNDC5

Last update 08 May 2025

Basic Info

Synonyms

EndoPDI, Endoplasmic reticulum resident protein 46, ER protein 46

+ [11]

Introduction

Protein disulfide isomerase of the endoplasmic reticulum lumen involved in the formation of disulfide bonds in proteins. Can reduce insulin disulfide bonds.

Drugs associated with TXNDC5

US20250066793

Patent Mining

Target

TXNDC5

Mechanism-

Active Org.

Development Center for Biotechnology

Originator Org.

Development Center for Biotechnology

Active Indication

Arthritis [+8]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TXNDC5

100 Translational Medicine associated with TXNDC5

0 Patents (Medical) associated with TXNDC5

159

Literatures (Medical) associated with TXNDC5

01 Apr 2025·Reproduction

Deletion of TXNDC5 downregulates TGFβ1-αSMA-mediated testicular fibrosis in mice

Article

Author: Chiang, Yi-Min ; Yang, Ya-Yi ; Tsai, Pei-Shiue ; Yang, Kai-Chien

Testicular torsion is a urological emergency. Delayed diagnosis and treatment hamper the testicular salvage rate and the subsequent recovery of the fertility. Although detorsion surgery restores the testicular blood flow, the process of torsion/detorsion leads to ischemia/reperfusion injury, which aggravates the primary damage due to the excessive generation of free radicals that disrupt antioxidant homeostasis. In the present study, we investigated the role of endoplasmic reticulum protein, thioredoxin domain-containing protein 5, in ischemia/reperfusion-induced testicular fibrosis. We showed that apart from disrupted testicular structure, elevated transforming growth factor beta 1, alpha-smooth muscle actin, and collagen type 1 protein expression accompanied by TXNDC5 upregulation were detected in mice that underwent ischemia/reperfusion injury. By Txndc5 deletion, fibrosis, redox oxidation, and extracellular matrix-associated signaling pathways and their accompanied genes/proteins were downregulated, indicating amelioration of testicular tissue damage and fibrosis in Txndc5-/- mice. With the apparent restoration of testicular structure and spermatogenesis, our study provides a potential therapeutic strategy by targeting TXNDC5 in testicular torsion patients to reduce ischemia/reperfusion-induced testicular fibrosis and to restore their fertility.

01 Mar 2025·Current Problems in Cardiology

The role and mechanism of TXNDC5 in cardio-oncology: Killing two birds with one stone?

Review

Author: Xing, Yanwei ; Shang, Hongcai ; Kong, YiFan ; Lin, Hongyuan ; Yang, Xinyu ; Zhang, Xiaoyu ; Dai, Qianqian ; An, Na ; Xu, Qianqian ; Li, Xiao ; Han, Songjie

Cardio-oncology has emerged as a new translational and clinical field owing to the growing repertory of cancer therapy. To date, there is a lack of effective pharmacological therapy to target cardiotoxicity. Cardio-oncology, which began by investigating the negative effects of cancer medicines on cardiovascular system, has since grown to include research into the similarities between cardiovascular disease (CVD) and cancer. Thioredoxin domain-containing protein 5 (TXNDC5) belongs to the protein disulfide isomerase (PDI) family. Many diseases, including CVD and cancer, improperly express TXNDC5. This review provides a comprehensive analysis of the expression patterns of TXNDC5 in diseases. It outlines the processes via which TXNDC5 contributes to the advancement of malignant diseases such as CVD and cancer. Additionally, it summarizes prospective therapeutic approaches that can be used to target TXNDC5 for the treatment of these diseases. This will offer novel perspectives for enhancing anticancer therapy and advancing cardio-oncology research and drug development.

01 Feb 2025·Research and Practice in Thrombosis and Haemostasis

Thiol isomerase ERp18 enhances platelet activation and arterial thrombosis

Article

Author: Han, Yue ; Jiang, Miao ; He, Chao ; Lv, Keyu ; Zhang, Jingyu ; Wu, Depei ; Wu, Yi ; Fang, Chao ; Zhao, Zhenzhen ; Yang, Aizhen ; Lu, Yi ; Zhang, Yuxin

BackgroundThiol isomerases regulate the thiol-disulfide exchange of functional proteins in cells. Using genetically modified mouse models and inhibitors, we and others demonstrated that 7 thiol isomerases (ERp57, protein diisulfide isomerase, ERp72, ERp46, ERp5, TMX4, and TMX1) participate in thrombosis. There are 21 thiol isomerases in mammals, but whether other enzymes of this family also contribute to thrombosis remains unknown.ObjectivesInvestigate whether and how ERp18 participates in arterial thrombosis.MethodsERp18 knockout mice and arterial thrombosis models were used to determine the role of ERp18 in thrombosis. Platelets from ERp18 knockout mice were used to detect aggregation, activation, spreading, and clot retraction. Finally, flow cytometry and immunoprecipitation were used to detect the binding between ERp18 and α_IIbβ₃.ResultsThe mice lacking ERp18 exhibited a prolonged tail bleeding time and decreased platelet thrombus formation in FeCl₃-induced carotid arterial injury and laser-induced cremaster artery injury models. ERp18 deficiency inhibited platelet aggregation, adenosine triphosphate release, integrin α_IIbβ₃ activation, P-selectin expression, platelet adhesion, as well as clot retraction. Flow cytometry and coimmunoprecipitation analyses revealed that ERp18 binds to the platelet surface via interaction with integrin α_IIbβ₃. Moreover, the ERp18 protein promoted the binding of integrin α_IIbβ₃ to fibrinogen and platelet aggregation. Furthermore, the recombinant ERp18 protein exhibited reductase activity and cleaved integrin α_IIbβ₃ disulfides.ConclusionERp18 participates in platelet activation and thrombosis. Its function is, at least in part, through the regulation of integrin α_IIbβ₃ function. This finding expands our understanding of the role of thiol isomerases in the redox regulation of thrombosis and platelet function.

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TXNDC5

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