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Critical protein GAPDH and its regulatory mechanisms in cancer cells

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), initially identified as a glycolytic enzyme and considered as a housekeeping gene, is widely used as an internal control in experiments on proteins, mRNA, and DNA. However, emerging evidence indicates that GAPDH is implicated in diverse functions ind...

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Autores principales: Zhang, Jin-Ying, Zhang, Fan, Hong, Chao-Qun, Giuliano, Armando E., Cui, Xiao-Jiang, Zhou, Guang-Ji, Zhang, Guo-Jun, Cui, Yu-Kun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Chinese Anti-Cancer Association 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383849/
https://www.ncbi.nlm.nih.gov/pubmed/25859407
http://dx.doi.org/10.7497/j.issn.2095-3941.2014.0019
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author Zhang, Jin-Ying
Zhang, Fan
Hong, Chao-Qun
Giuliano, Armando E.
Cui, Xiao-Jiang
Zhou, Guang-Ji
Zhang, Guo-Jun
Cui, Yu-Kun
author_facet Zhang, Jin-Ying
Zhang, Fan
Hong, Chao-Qun
Giuliano, Armando E.
Cui, Xiao-Jiang
Zhou, Guang-Ji
Zhang, Guo-Jun
Cui, Yu-Kun
author_sort Zhang, Jin-Ying
collection PubMed
description Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), initially identified as a glycolytic enzyme and considered as a housekeeping gene, is widely used as an internal control in experiments on proteins, mRNA, and DNA. However, emerging evidence indicates that GAPDH is implicated in diverse functions independent of its role in energy metabolism; the expression status of GAPDH is also deregulated in various cancer cells. One of the most common effects of GAPDH is its inconsistent role in the determination of cancer cell fate. Furthermore, studies have described GAPDH as a regulator of cell death; other studies have suggested that GAPDH participates in tumor progression and serves as a new therapeutic target. However, related regulatory mechanisms of its numerous cellular functions and deregulated expression levels remain unclear. GAPDH is tightly regulated at transcriptional and posttranscriptional levels, which are involved in the regulation of diverse GAPDH functions. Several cancer-related factors, such as insulin, hypoxia inducible factor-1 (HIF-1), p53, nitric oxide (NO), and acetylated histone, not only modulate GAPDH gene expression but also affect protein functions via common pathways. Moreover, posttranslational modifications (PTMs) occurring in GAPDH in cancer cells result in new activities unrelated to the original glycolytic function of GAPDH. In this review, recent findings related to GAPDH transcriptional regulation and PTMs are summarized. Mechanisms and pathways involved in GAPDH regulation and its different roles in cancer cells are also described.
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spelling pubmed-43838492015-04-09 Critical protein GAPDH and its regulatory mechanisms in cancer cells Zhang, Jin-Ying Zhang, Fan Hong, Chao-Qun Giuliano, Armando E. Cui, Xiao-Jiang Zhou, Guang-Ji Zhang, Guo-Jun Cui, Yu-Kun Cancer Biol Med Review Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), initially identified as a glycolytic enzyme and considered as a housekeeping gene, is widely used as an internal control in experiments on proteins, mRNA, and DNA. However, emerging evidence indicates that GAPDH is implicated in diverse functions independent of its role in energy metabolism; the expression status of GAPDH is also deregulated in various cancer cells. One of the most common effects of GAPDH is its inconsistent role in the determination of cancer cell fate. Furthermore, studies have described GAPDH as a regulator of cell death; other studies have suggested that GAPDH participates in tumor progression and serves as a new therapeutic target. However, related regulatory mechanisms of its numerous cellular functions and deregulated expression levels remain unclear. GAPDH is tightly regulated at transcriptional and posttranscriptional levels, which are involved in the regulation of diverse GAPDH functions. Several cancer-related factors, such as insulin, hypoxia inducible factor-1 (HIF-1), p53, nitric oxide (NO), and acetylated histone, not only modulate GAPDH gene expression but also affect protein functions via common pathways. Moreover, posttranslational modifications (PTMs) occurring in GAPDH in cancer cells result in new activities unrelated to the original glycolytic function of GAPDH. In this review, recent findings related to GAPDH transcriptional regulation and PTMs are summarized. Mechanisms and pathways involved in GAPDH regulation and its different roles in cancer cells are also described. Chinese Anti-Cancer Association 2015-03 /pmc/articles/PMC4383849/ /pubmed/25859407 http://dx.doi.org/10.7497/j.issn.2095-3941.2014.0019 Text en 2015 Cancer Biology & Medicine This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/
spellingShingle Review
Zhang, Jin-Ying
Zhang, Fan
Hong, Chao-Qun
Giuliano, Armando E.
Cui, Xiao-Jiang
Zhou, Guang-Ji
Zhang, Guo-Jun
Cui, Yu-Kun
Critical protein GAPDH and its regulatory mechanisms in cancer cells
title Critical protein GAPDH and its regulatory mechanisms in cancer cells
title_full Critical protein GAPDH and its regulatory mechanisms in cancer cells
title_fullStr Critical protein GAPDH and its regulatory mechanisms in cancer cells
title_full_unstemmed Critical protein GAPDH and its regulatory mechanisms in cancer cells
title_short Critical protein GAPDH and its regulatory mechanisms in cancer cells
title_sort critical protein gapdh and its regulatory mechanisms in cancer cells
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383849/
https://www.ncbi.nlm.nih.gov/pubmed/25859407
http://dx.doi.org/10.7497/j.issn.2095-3941.2014.0019
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