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Cited by 1,480Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsCancer and biochemical research

Cell transformation by the superoxide-generating oxidase Mox1

Suh, Young-Ah, Arnold, Rebecca S., Lassegue, Bernard, Shi, Jing, Xu, Xiangxi, Sorescu, Dan, Chung, Andrew B., Griendling, Kathy K. +1 more·1999·Nature
DOI 10.1038/43459
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Abstract

Reactive oxygen species (ROS) generated in some non-phagocytic cells are implicated in mitogenic signalling and cancer. Many cancer cells show increased production of ROS, and normal cells exposed to hydrogen peroxide or superoxide show increased proliferation and express growth-related genes. ROS are generated in response to growth factors, and may affect cell growth, for example in vascular smooth-muscle cells. Increased ROS in Ras-transformed fibroblasts correlates with increased mitogenic rate. Here we describe the cloning of mox1, which encodes a homologue of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. mox1 messenger RNA is expressed in colon, prostate, uterus and vascular smooth muscle, but not in peripheral blood leukocytes. In smooth-muscle cells, platelet-derived growth factor induces mox1 mRNA production, while antisense mox1 mRNA decreases superoxide generation and serum-stimulated growth. Overexpression of mox1 in NIH3T3 cells increases superoxide generation and cell growth. Cells expressing mox1 have a transformed appearance, show anchorage-independent growth and produce tumours in athymic mice. These data link ROS production by Mox1 to growth control in non-phagocytic cells.

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  • Nox1 is predominantly expressed in colon epithelium but also detected in other peripheral tissues, including dorsal root ganglia and vascular cells.

    “Nox1 is predominantly expressed in colon epithelium, but was also detected in other peripheral tissues, including dorsal root ganglia and in vascular cells (Suh et al., 1999;Bedard and Krause, 2007;Ibi et al., 2008).”

    From Neurotoxic Activation of Microglia Is Promoted by a Nox1-Dependent NADPH Oxidase (2008) · cites this paper as Suh et al., 1999

  • Elevation of reactive metabolites can support oncogenesis in some contexts.

    “While elevation of reactive metabolites can support oncogenesis in some contexts (Arnold et al., 2001; Irani et al., 1997; Suh et al., 1999; Weinberg et al., 2010), at high levels reactive metabolites become toxic and kill cells due to the resulting damage to the proteome and genome (Karisch et al., 2011; Rabbani and Thornalley, 2014).”

    From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Suh et al., 1999

  • Thioredoxin has been proposed to deglutathionylate eNOS independently of glutathione oxidation.

    “Along with glutaredoxin-1, thioredoxin has also been proposed to deglutathionylate eNOS, and this process is independent of glutathione oxidation (907).”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [907]

  • The discovery of the first antioxidant enzymes (superoxide dismutase) came decades before the discovery that non-phagocytic cells also possess enzymes (NADPH oxidases) whose sole biological function is to produce ROS.

    “First, the discovery of the first antioxidant enzymes (superoxide dismutase) came decades before the discovery that non-phagocytic cells also possess enzymes (NADPH oxidases) whose sole biological function is to produce ROS 78, 79.”

    From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [79]

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Authors
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D.
Affiliations
Emory University (US)
Corresponding author
Lambeth, J. David
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1999-09
Volume
401
Issue
6748
Pages
79-82
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/43459
OpenAlex
W2101745219
Cited by
1,480
References
30
Citations by year
2026: 10 · 2025: 15 · 2024: 24 · 2023: 31 · 2022: 19 · 2021: 23 · 2020: 34 · 2019: 33 · 2018: 19 · 2017: 39 · 2016: 42 · 2015: 47 · 2014: 50 · 2013: 59 · 2012: 48
FWCI
25.72
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Funders
National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
Keywords
NADPH oxidase, gp91phox, reactive oxygen species, cell transformation, mitogenic signaling, platelet-derived growth factor, vascular smooth muscle cells, cell proliferation, anchorage-independent growth, carcinogenesis, non-phagocytic cells, ras-transformed fibroblasts
MeSH terms
NADPH Oxidase 2, Aconitate Hydratase, Amino Acid Sequence, Animals, Catalysis, Cell Line, Cell Transformation, Neoplastic, Cloning, Molecular, Colon, Humans, Membrane Glycoproteins, Mice, Nude, Molecular Sequence Data, NADH, NADPH Oxidoreductases, RNA, Messenger, Superoxides, Tissue Distribution, Transfection, 3T3 Cells, Reactive Oxygen Species, Sequence Homology, Amino Acid, NADPH Oxidases, Mice, Rats

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