TXNDC5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology

Horna-Terrón, E. ; Pradilla-Dieste, A. ; Sánchez-de-Diego, C. ; Osada, J. (Universidad de Zaragoza)

Resumen: 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.

Idioma: Inglés

DOI: 10.3390/ijms151223501

Año: 2014

Publicado en: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 15, 12 (2014), 23501-23518
ISSN: 1661-6596

Factor impacto JCR: 2.862 (2014)

Categ. JCR: CHEMISTRY, MULTIDISCIPLINARY rank: 45 / 154 = 0.292 (2014) - Q2 - T1
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 134 / 290 = 0.462 (2014) - Q2 - T2

Financiación: info:eu-repo/grantAgreement/ES/CICYT-FEDER/2013-41651-R
Financiación: info:eu-repo/grantAgreement/ES/DGA/B69
Financiación: info:eu-repo/grantAgreement/ES/MICINN/SAF010-14958

Tipo y forma: Article (Published version)

Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)