TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology
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 o...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2014-12-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | http://www.mdpi.com/1422-0067/15/12/23501 |
id |
doaj-a8e6fcd9bc334dd28cd0ab30db237ba3 |
---|---|
record_format |
Article |
spelling |
doaj-a8e6fcd9bc334dd28cd0ab30db237ba32020-11-24T22:49:51ZengMDPI AGInternational Journal of Molecular Sciences1422-00672014-12-011512235012351810.3390/ijms151223501ijms151223501TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and PathologyElena Horna-Terrón0Alberto Pradilla-Dieste1Cristina Sánchez-de-Diego2Jesús Osada3Grado de Biotecnología, Universidad de Zaragoza, Zaragoza E-50013, SpainGrado de Biotecnología, Universidad de Zaragoza, Zaragoza E-50013, SpainGrado de Biotecnología, Universidad de Zaragoza, Zaragoza E-50013, SpainDepartamento Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón (IIS), Universidad de Zaragoza, Zaragoza E-50013, SpainThioredoxin 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.http://www.mdpi.com/1422-0067/15/12/23501thioredoxin domain containing 5 (TXNDC5)protein disulfide isomerase (PDI)endoplasmic reticulum 46 (Erp46)PDI15thioredoxin-related protein in the cell plasma (PC-TRP)endo PDI |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Elena Horna-Terrón Alberto Pradilla-Dieste Cristina Sánchez-de-Diego Jesús Osada |
spellingShingle |
Elena Horna-Terrón Alberto Pradilla-Dieste Cristina Sánchez-de-Diego Jesús Osada TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology International Journal of Molecular Sciences 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 |
author_facet |
Elena Horna-Terrón Alberto Pradilla-Dieste Cristina Sánchez-de-Diego Jesús Osada |
author_sort |
Elena Horna-Terrón |
title |
TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology |
title_short |
TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology |
title_full |
TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology |
title_fullStr |
TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology |
title_full_unstemmed |
TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology |
title_sort |
txndc5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2014-12-01 |
description |
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. |
topic |
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 |
url |
http://www.mdpi.com/1422-0067/15/12/23501 |
work_keys_str_mv |
AT elenahornaterron txndc5anewlydiscovereddisulfideisomerasewithakeyroleincellphysiologyandpathology AT albertopradilladieste txndc5anewlydiscovereddisulfideisomerasewithakeyroleincellphysiologyandpathology AT cristinasanchezdediego txndc5anewlydiscovereddisulfideisomerasewithakeyroleincellphysiologyandpathology AT jesusosada txndc5anewlydiscovereddisulfideisomerasewithakeyroleincellphysiologyandpathology |
_version_ |
1725674791895040000 |