TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology

• Main Authors: Elena Horna-Terrón, Alberto Pradilla-Dieste, Cristina Sánchez-de-Diego, Jesús Osada
• Format: Article
• Language: English
• Published: MDPI AG 2014-12-01
• Series: International Journal of Molecular Sciences
• Subjects: thioredoxin domain containing 5 (TXNDC5); protein disulfide isomerase (PDI); endoplasmic reticulum 46 (Erp46); PDI15; thioredoxin-related protein in the cell plasma (PC-TRP); endo PDI
• Online Access: http://www.mdpi.com/1422-0067/15/12/23501

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.