TMX2

Last update 08 May 2025

Basic Info

Synonyms

Cell proliferation-inducing gene 26 protein, PDIA12, Thioredoxin domain-containing protein 14

+ [4]

Introduction

Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain.

100 Clinical Results associated with TMX2

100 Translational Medicine associated with TMX2

0 Patents (Medical) associated with TMX2

Literatures (Medical) associated with TMX2

01 Feb 2025·Heliyon

Potential and mechanisms of indigenous Indonesian medicinal plants in treating sexual dysfunction: A systematic review and pharmacological network overview

Article

Author: Sukardiman ; Handayani, Rosita ; Mutiah, Roihatul

The epidemiology of Erectile Dysfunction (ED) continues to exhibit an increasing trend annually. The use of synthetic drugs in treating ED often leads to undesirable side effects and has limited efficacy. In Indonesia, several indigenous plants have been empirically utilized for ED remediation. This study aims to identify the latest scientific evidence on the potential of native Indonesian medicinal plants for ED treatment and elucidate the underlying molecular mechanisms using a systematic review and Pharmacological Network approach. There are 12 potential plants most commonly used by ethnic groups in Indonesia to treat erectile dysfunction (ED) as reviewed in this study. A systematic review search was conducted across three databases (PubMed, Scopus, and Springer) without limiting the publication years. Article screening was performed using the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) flowchart. Determination of compound target genes was carried out using GeneCards, while disease target genes were analyzed using DisGeNET. Network topology was explored with Cytoscape 3.10, and the construction of Protein-Protein Interaction Networks was realized using STRING version 12.0. GO and KEGG analyses were subsequently conducted with SRplot. The systematic review findings indicated that 12 articles met the predefined inclusion criteria. The pharmacology network analysis demonstrated that the compounds present in Eurycoma longifolia, specifically stigmasterol, eurycomanone, and eurycomalactone, target 13 genes associated with erectile dysfunction (ED), which include BCL2, AKT1, SOAT1, PCSK9, ACHE, BDNF-AS, TMX2-CTNND1, GSK3B, LINCO1672, TP53, H19, HIF1A, and IL1B. These target genes are connected to the biological mechanisms underlying steroid hormone biosynthesis, which is essential for the formation of testosterone. Therefore, Eurycoma longifolia demonstrates significant potential for development as a promising phytopharmaceutical candidate in the treatment of sexual dysfunction.

01 Dec 2024·Life Science Alliance

TMX5/TXNDC15, a natural trapping mutant of the PDI family is a client of the proteostatic factor ERp44

Article

Author: Soldà, Tatiana ; Guerra, Concetta ; Hoefner, Carolin ; Molinari, Maurizio ; Galli, Carmela

The ER is the organelle of nucleated cells that produces lipids, sugars, and proteins. More than 20 ER-resident members of the protein disulfide isomerase (PDI) family regulate formation, isomerization, and disassembly of covalent bonds in newly synthesized polypeptides. The PDI family includes few membrane-bound members. Among these, TMX1, TMX2, TMX3, TMX4, and TMX5 belong to the thioredoxin-related transmembrane (TMX) protein family. TMX5 is the least-known member of the family. Here, we establish that TMX5 covalently engages via its active site cysteine residue at position 220 a subset of secretory proteins, mainly single- and multipass Golgi-resident polypeptides. TMX5 also interacts non-covalently, and covalently, via non-catalytic cysteine residues, with the PDI family members PDI, ERp57, and ERp44. The association between TMX5 and ERp44 requires formation of a mixed disulfide between the catalytic cysteine residue 29 of ERp44 and the non-catalytic cysteine residues 114 and/or 124 of TMX5 and controls the ER localization of TMX5 in pre-Golgi compartments. Thus, TMX5 belongs to the family of proteins including Ero1α, Ero1β, Prx4, ERAP1, and SUMF1 that operate in pre-Golgi compartments but lack localization sequences required to position themselves and rely on ERp44 engagement for proper intercompartmental distribution.

01 Nov 2024·Veterinary Microbiology

The modulation of proteomics and antioxidant stress is involved in the effect of nitazoxanide against Japanese encephalitis virus in vitro

Article

Author: Xiong, Chengeng ; Zhang, Keyu ; Zhou, Donghai ; Su, Yu ; Wang, Xiaoyang ; Wang, Chunmei ; Wang, Yanping ; Zhou, Wen

Japanese encephalitis virus (JEV) is a significant circulating arbovirus flavivirus and the primary cause of viral encephalitis in Asia. Previous studies have demonstrated that nitazoxanide (NTZ), an antiparasitic gastroenteritis medication classified as a thiazolide, exhibits efficacy against JEV both in vitro and in vivo. To explore the potential antiviral mechanisms, we employed Tandem Mass Tag (TMT)-based quantitative proteomics to identify differentially expressed proteins (DEPs) among three groups: Blank cell group, JEV-infected cell group, and JEV-infected cells treated with NTZ. Our analysis revealed that NTZ treatment led to the upregulation of 30 DEPs and downregulation of 54 DEPs in JEV-infected cells. Enrichment analysis using Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) indicated that these DEPs are involved in various biological processes and signaling pathways, including transport, localization, response to wounding, P53 pathway activation, and fatty acid metabolism-related pathways. Moreover, we observed that the expression trend of TMX2, a protein associated with redox homeostasis, was consistent with findings from TMT-based quantitative proteomics. Further investigations into reactive oxygen species (ROS), mitochondrial membrane potential, antioxidant enzyme activity, and the KEAP1-NRF2 pathway demonstrated that NTZ effectively regulates the KEAP1-NRF2 pathway while suppressing oxidative stress induced by JEV infection. In conclusion, the proteomic data along with antioxidant stress results presented herein provide a foundational basis for further research into the molecular mechanisms and potential targets of NTZ against JEV.

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TMX2

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