A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development

Hedy A. Chawsheen; Qi Ying; Hong Jiang; Qiou Wei

doi:10.1016/j.gendis.2018.09.003

A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development

Hedy A. Chawsheen
, Qi Ying
, Hong Jiang
, Qiou Wei

Toxicology and Cancer Biology

Research output: Contribution to journal › Review article › peer-review

48 Scopus citations

Abstract

Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family. As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found overexpressed in specimens of many human diseases including various types of cancer. In this review, we summarized the biochemical function of TXNDC5 in mammalian cells and the recent progress on the understanding of its role and molecular mechanisms in cancer development. Findings of TXNDC5 in the activation of intracellular signaling pathways, stimulation of cell growth & proliferation, facilitation of cell survival and modulation of extracellular matrix to affect cancer cell invasion and metastasis are reviewed. These published studies suggest that strategies of targeting TXNDC5 can be developed as potentially valuable methods for the treatment of certain types of cancer in patients.

Original language	English
Pages (from-to)	312-322
Number of pages	11
Journal	Genes and Diseases
Volume	5
Issue number	4
DOIs	https://doi.org/10.1016/j.gendis.2018.09.003
State	Published - Dec 2018

Bibliographical note

Publisher Copyright:
© 2018 Chongqing Medical University

Funding

This work was partially supported by the National Institutes of Health (NCI grant number R01CA222596 ), Department of Defense (grant number W81XWH-16-1-0203 ), American Cancer Society (grant number RSG-16-213-01-TBE ) and Kentucky Lung Cancer Research Program ( KLCRP2016 ). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health or other funding agencies.

Funders	Funder number
Kentucky Lung Cancer Research Program	KLCRP2016
National Institutes of Health (NIH)
U.S. Department of Defense	W81XWH-16-1-0203
American Cancer Society-Michigan Cancer Research Fund	RSG-16-213-01-TBE
National Childhood Cancer Registry – National Cancer Institute	R01CA222596

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Cancer
Cell signal
Protein disulfide isomerase
Protein folding
Receptor modulation

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Genetics(clinical)
Cell Biology

Access to Document

10.1016/j.gendis.2018.09.003

Cite this

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title = "A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development",

abstract = "Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family. As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found overexpressed in specimens of many human diseases including various types of cancer. In this review, we summarized the biochemical function of TXNDC5 in mammalian cells and the recent progress on the understanding of its role and molecular mechanisms in cancer development. Findings of TXNDC5 in the activation of intracellular signaling pathways, stimulation of cell growth \& proliferation, facilitation of cell survival and modulation of extracellular matrix to affect cancer cell invasion and metastasis are reviewed. These published studies suggest that strategies of targeting TXNDC5 can be developed as potentially valuable methods for the treatment of certain types of cancer in patients.",

keywords = "Cancer, Cell signal, Protein disulfide isomerase, Protein folding, Receptor modulation",

author = "Chawsheen, \{Hedy A.\} and Qi Ying and Hong Jiang and Qiou Wei",

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year = "2018",

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doi = "10.1016/j.gendis.2018.09.003",

language = "English",

volume = "5",

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T1 - A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development

AU - Chawsheen, Hedy A.

AU - Ying, Qi

AU - Jiang, Hong

AU - Wei, Qiou

PY - 2018/12

Y1 - 2018/12

N2 - Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family. As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found overexpressed in specimens of many human diseases including various types of cancer. In this review, we summarized the biochemical function of TXNDC5 in mammalian cells and the recent progress on the understanding of its role and molecular mechanisms in cancer development. Findings of TXNDC5 in the activation of intracellular signaling pathways, stimulation of cell growth & proliferation, facilitation of cell survival and modulation of extracellular matrix to affect cancer cell invasion and metastasis are reviewed. These published studies suggest that strategies of targeting TXNDC5 can be developed as potentially valuable methods for the treatment of certain types of cancer in patients.

AB - Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family. As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found overexpressed in specimens of many human diseases including various types of cancer. In this review, we summarized the biochemical function of TXNDC5 in mammalian cells and the recent progress on the understanding of its role and molecular mechanisms in cancer development. Findings of TXNDC5 in the activation of intracellular signaling pathways, stimulation of cell growth & proliferation, facilitation of cell survival and modulation of extracellular matrix to affect cancer cell invasion and metastasis are reviewed. These published studies suggest that strategies of targeting TXNDC5 can be developed as potentially valuable methods for the treatment of certain types of cancer in patients.

KW - Cancer

KW - Cell signal

KW - Protein disulfide isomerase

KW - Protein folding

KW - Receptor modulation

UR - https://www.scopus.com/pages/publications/85055507903

UR - https://www.scopus.com/pages/publications/85055507903#tab=citedBy

U2 - 10.1016/j.gendis.2018.09.003

DO - 10.1016/j.gendis.2018.09.003

M3 - Review article

AN - SCOPUS:85055507903

SN - 2352-4820

VL - 5

SP - 312

EP - 322

JO - Genes and Diseases

JF - Genes and Diseases

IS - 4

ER -

A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development

Abstract

Bibliographical note

Funding

UN SDGs

Keywords

ASJC Scopus subject areas

Access to Document

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