The mechanism by which reactive oxygen species (ROS) are produced by tumour cells remained incompletely understood until the discovery over the last 15 years of the family of NADPH oxidases (NOXs 1–5 and dual oxidases DUOX1/2) which are structural homologues of gp91phox, the major membrane-bound component of the respiratory burst oxidase of leucocytes. Knowledge of the roles of the NOX isoforms in cancer is rapidly expanding. Recent evidence suggests that both NOX1 and DUOX2 species produce ROS in the gastrointestinal tract as a result of chronic inflammatory stress; cytokine induction (by interferon-γ, tumour necrosis factor α, and interleukins IL-4 and IL-13) of NOX1 and DUOX2 may contribute to the development of colorectal and pancreatic carcinomas in patients with inflammatory bowel disease and chronic pancreatitis, respectively. NOX4 expression is increased in pre-malignant fibrotic states which may lead to carcinomas of the lung and liver. NOX5 is highly expressed in malignant melanomas, prostate cancer and Barrett's oesophagus-associated adenocarcinomas, and in the last it is related to chronic gastro-oesophageal reflux and inflammation. Over-expression of functional NOX proteins in many tissues helps to explain tissue injury and DNA damage from ROS that accompany pre-malignant conditions, as well as elucidating the potential mechanisms of NOX-related damage that contribute to both the initiation and the progression of a wide range of solid and haematopoietic malignancies.
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Review Article|
March 27 2015
NADPH oxidases and cancer
Krishnendu Roy;
Krishnendu Roy
*Division of Cancer Treatment and Diagnosis, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Yongzhong Wu;
Yongzhong Wu
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Jennifer L. Meitzler;
Jennifer L. Meitzler
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Agnes Juhasz;
Agnes Juhasz
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Han Liu;
Han Liu
*Division of Cancer Treatment and Diagnosis, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Guojian Jiang;
Guojian Jiang
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Jiamo Lu;
Jiamo Lu
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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Smitha Antony;
Smitha Antony
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
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James H. Doroshow
*Division of Cancer Treatment and Diagnosis, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
†Developmental Therapeutics Branch of the Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
Correspondence: Dr James H. Doroshow (email [email protected]).
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Publisher: Portland Press Ltd
Received:
September 12 2014
Revision Received:
January 16 2015
Accepted:
February 05 2015
Online ISSN: 1470-8736
Print ISSN: 0143-5221
© The Authors Journal compilation © 2015 Biochemical Society
2015
Clin Sci (Lond) (2015) 128 (12): 863–875.
Article history
Received:
September 12 2014
Revision Received:
January 16 2015
Accepted:
February 05 2015
Citation
Krishnendu Roy, Yongzhong Wu, Jennifer L. Meitzler, Agnes Juhasz, Han Liu, Guojian Jiang, Jiamo Lu, Smitha Antony, James H. Doroshow; NADPH oxidases and cancer. Clin Sci (Lond) 1 June 2015; 128 (12): 863–875. doi: https://doi.org/10.1042/CS20140542
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