Year-end Sale % OFF 
Abstract
Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains. Moreover, it can also work as an electron transfer reaction, recovering the functional isoform of other protein disulfide isomerases, replacing reduced glutathione in its role. Finally, it also acts as a cellular adapter, interacting with the N-terminal domain of adiponectin receptor. As can be inferred from all these functions, TXNDC5 plays an important role in cell physiology; therefore, dysregulation of its expression is associated with oxidative stress, cell ageing and a large range of pathologies such as arthritis, cancer, diabetes, neurodegenerative diseases, vitiligo and virus infections. Its implication in all these important diseases has made TXNDC5 a susceptible biomarker or even a potential pharmacological target.
Highlights
The thioredoxin domain containing protein 5 (TXNDC5), known as resident endoplasmic reticulum 46 (Erp46); protein disulfide isomerase family A, member 15 (PDI15); thioredoxin-related protein in the cell plasma (PC-TRP) or endo PDI; is a protein-disulfide isomerase
The Thioredoxin domain-containing 5 (TXNDC5) gene encodes for six transcripts; while all are generated by alternative splicing, only two of them code for a protein (TXNDC5-001 and TXNDC5-003) [17]
TXNDC5 is a member of the disulfide isomerase (PDI) family [22], mainly expressed in liver and endothelial cells [1,23]
Summary
The thioredoxin domain containing protein 5 (TXNDC5), known as resident endoplasmic reticulum 46 (Erp46); protein disulfide isomerase family A, member 15 (PDI15); thioredoxin-related protein in the cell plasma (PC-TRP) or endo PDI; is a protein-disulfide isomerase. Due to the anaerobic metabolism of cancer cells [4], it has been stated that their proliferation could be due to hypoxia and this would induce TXNDC5. This notion has been supported by studies in various diseases in which oxygen is limited, such as diabetes [9], arthritis [10,11,12], neurodegenerative diseases [13] and vitiligo [14]. In non-small cell lung carcinoma, hypoxia does not change TXNDC5 expression [7], leaving an open horizon to better characterize its regulation. This wide spectrum of changes and controversies warrants further research in the future. The combined information of the two sources has been the basis of this review
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
