TXNDC5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology.
TXNDC5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology.
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DOI：
10.3390/ijms151223501
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发表时间：
2014-12-17
影响因子：
5.6
通讯作者：
Osada J
中科院分区：
文献类型：
--
作者：
Horna-Terrón E;Pradilla-Dieste A;Sánchez-de-Diego C;Osada J
含硫氧还蛋白结构域5(TXNDC5)是蛋白质二硫键异构酶家族的一员，在尚未完全确定的条件下作为内质网的伴侣，与多种细胞蛋白相互作用，通过其硫氧还蛋白结构域促进蛋白质的正确折叠和二硫键的正确形成。此外，它还可以作为电子转移反应，恢复其他蛋白质二硫键异构酶的功能异构体，取代还原型谷胱甘肽的作用。最后，它还起到细胞适配器的作用，与脂联素受体的N末端区域相互作用。从所有这些功能可以推断，TXNDC5在细胞生理学中起着重要的作用；因此，它的表达异常与氧化应激、细胞衰老和一系列的病理变化有关，如关节炎、癌症、糖尿病、神经退行性疾病、白癜风和病毒感染。它在所有这些重要疾病中的作用使TXNDC5成为一个敏感的生物标志物，甚至是一个潜在的药理靶点。
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.
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