Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1
Open accessAbstract
Nox1, a homologue of gp91 phox , the catalytic moiety of the superoxide (O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{-}}}\end{equation*}\end{document} )-generating NADPH oxidase of phagocytes, causes increased O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{-}}}\end{equation*}\end{document} generation, increased mitotic rate, cell transformation, and tumorigenicity when expressed in NIH 3T3 fibroblasts. This study explores the role of reactive oxygen species (ROS) in regulating cell growth and transformation by Nox1. H 2 O 2 concentration increased ≈10-fold in Nox1-expressing cells, compared with <2-fold increase in O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{-}}}\end{equation*}\end{document} . When human catalase was expressed in Nox1-expressing cells, H 2 O 2 concentration decreased, and the cells reverted to a normal appearance, the growth rate normalized, and cells no longer produced tumors in athymic mice. A large number of genes, including many related to cell cycle, growth, and cancer (but unrelated to oxidative stress), were expressed in Nox1-expressing cells, and more than 60% of these returned to normal levels on coexpression of catalase. Thus, H 2 O 2 in low concentrations functions as an intracellular signal that triggers a genetic program related to cell growth.
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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 Arnold et al., 2001
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Cites
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504 · see citing works
Blake, M. S., Johnston, K. H., Russell-Jones, G. J., & Gotschlich, E. C. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90320-8 · Cited by 2,136 · see citing works
Antiangiogenic therapy of experimental cancer does not induce acquired drug resistance
Boehm, T., Folkman, J., Browder, T., & O'Reilly, M. S. (1997) · Nature · doi:10.1038/37126 · Cited by 1,683 · see citing works
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588 · see citing works
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480 · see citing works
Self-citationOxidative stress and gene regulation
Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,297 · see citing works
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works
Finkel, T. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80147-6 · Cited by 1,170 · see citing works
Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,166 · see citing works
Storz, G., & Imlayt, J. A. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80033-2 · Cited by 1,077 · see citing works
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
Schulze‐Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., & Fiers, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42768-8 · Cited by 935 · see citing works
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840 · see citing works
Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family
Deken, X. D., Wang, D., Many, M., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., & Miot, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000916200 · Cited by 639 · see citing works
Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells
Carter, W. O., Naryanan, P. K., & Robinson, J. P. (1994) · Journal of Leukocyte Biology · doi:10.1002/jlb.55.2.253 · Cited by 636 · see citing works
Modulation of fibroblast proliferation by oxygen free radicals
Murrell, G. A. C., Francis, M. J. O., & Bromley, L. (1990) · Biochemical Journal · doi:10.1042/bj2650659 · Cited by 625 · see citing works
Activation of the JAK-STAT pathway by reactive oxygen species
Simon, A. R., Rai, U., Fanburg, B. L., & Cochran, B. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.6.c1640 · Cited by 600 · see citing works
The H2O2 Stimulon in Saccharomyces cerevisiae
Godon, C., Lagniel, G., Lee, J., Buhler, J., Kieffer‐Jaquinod, S., Perrot, M., Boucherie, H., Tolédano, M. B., & Labarre, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22480 · Cited by 566 · see citing works
Church, S. L., Grant, J. W., Ridnour, L. A., Oberley, L. W., Swanson, P. E., Meltzer, P. S., & Trent, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.3113 · Cited by 474 · see citing works
Enzymic mechanisms of superoxide production
Cross, A. R., & Jones, O. T. G. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80140-9 · Cited by 468 · see citing works
Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase
Dupuy, C., Ohayon, R., Valent, A., Noël‐Hudson, M., Dème, D., & Virion, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37265 · Cited by 464 · see citing works
Schmidt, K. N., Amstad, P., Cerutti, P., & Baeuerle, P. A. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90076-4 · Cited by 454 · see citing works
Williams, M. D., Remmen, H. V., Conrad, C. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28510 · Cited by 453 · see citing works
Morgan, R. W., Christman, M. F., Jacobson, F. S., Storz, G., & Ames, B. N. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8059 · Cited by 420 · see citing works
Redox modulation of p53 conformation and sequence-specific DNA binding in vitro.
Hainaut, P. L., & Milner, J. (1993) · PubMed · Cited by 408 · see citing works
Lambeth, J. D., Cheng, G., Arnold, R. S., & Edens, W. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01658-3 · Cited by 355 · see citing works
Self-citationBarrett, W. C., DeGnore, J. P., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34543 · Cited by 355 · see citing works
Ruch, W., Cooper, P. H., & Baggiolini, M. (1983) · Journal of Immunological Methods · doi:10.1016/s0022-1759(83)80008-8 · Cited by 277 · see citing works
Redox signaling and gene control in the Escherichia coli soxRS oxidative stress regulon — a review
Demple, B. (1996) · Gene · doi:10.1016/s0378-1119(96)00329-0 · Cited by 239 · see citing works
de Haan, J. B., Cristiano, F., Iannello, R. C., Bladier, C., Kelner, M. J., & Kola, I. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.2.283 · Cited by 233 · see citing works
Wenk, J., Brenneisen, P., Wlaschek, M., Poswig, A., Briviba, K., Oberley, T. D., & Scharffetter‐Kochanek, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25869 · Cited by 224 · see citing works
Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide.
Natarajan, V., Taher, M. M., Roehm, B., Parinandi, N. L., Schmid, H. H. O., Kiss, Z., & Garcia, J. G. N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54023-0 · Cited by 211 · see citing works
Chen, Q. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06640.x · Cited by 176 · see citing works
Min, D. S., Kim, E., & Exton, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29986 · Cited by 174 · see citing works
Bladier, C., Wolvetang, E. J., Hutchinson, P. E., de Haan, J. B., & Kola, I. (1997) · PubMed · Cited by 168 · see citing works
BABIOR, B. M. (1995) · Current Opinion in Hematology · doi:10.1097/00062752-199502010-00008 · Cited by 157 · see citing works
Yan, T., Oberley, L. W., Zhong, W., & Clair, D. K. S. (1996) · PubMed · Cited by 154 · see citing works
Flow cytometric detection of hydrogen peroxide production induced by doxorubicin in cancer cells
Ubezio, P., & Civoli, F. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90129-5 · Cited by 152 · see citing works
Control of cell proliferation by reactive oxygen species
Burdon, R. H. (1996) · Biochemical Society Transactions · doi:10.1042/bst0241028 · Cited by 152 · see citing works
Hydrogen Peroxide Activates p70S6k Signaling Pathway
Bae, G., Seo, D. W., Kwon, H.-K., Lee, H. Y., Hong, S., Lee, Z., Ha, K., Lee, H. W., & Han, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32596 · Cited by 150 · see citing works
Reactive Oxygen Species Activate p90 Ribosomal S6 Kinase via Fyn and Ras
Abe, J., Okuda, M., Huang, Q., Yoshizumi, M., & Berk, B. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1739 · Cited by 141 · see citing works
A modified catalase assay suitable for a plate reader and for the analysis of brain cell cultures
Cohen, G., Kim, M., & Ogwu, V. (1996) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(96)00011-8 · Cited by 117 · see citing works
The NADPH Oxidase of Phagocytic Leukocytesa
Segal, A. W., & Shatwell, K. P. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb46249.x · Cited by 92 · see citing works
Effects of a biomimetic superoxide dismutase on complete and multistage carcinogenesis in mouse skin
Egner, P. A., & Kensler, T. W. (1985) · Carcinogenesis · doi:10.1093/carcin/6.8.1167 · Cited by 67 · see citing works
Fernandez‐Pol, J. A., Hamilton, P. D., & Klos, D. J. (1982) · PubMed · Cited by 65 · see citing works
Wartenberg, M., Diedershagen, H., Hescheler, J., & Sauer, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27759 · Cited by 56 · see citing works
Gansauge, S., Gansauge, F., Gause, H., Poch, B., Schoenberg, M. H., & Beger, H. G. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00059-8 · Cited by 55 · see citing works
Klockmann, M. T. U., Jahn, H., Hippenstiel, S., Krämer, H., & Suttorp, N. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199806)175:3 · Cited by 19 · see citing works
Shibanuma, M., Arata, S., Murata, M., et al. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1139 · Cited by 17 · see citing works
Flagged first, then by citations
Research works printed but not linked: 9
- [4]Bladier C, Wolvetang E J, Hutchinson P, de Haan J B, Kola I. Cell Growth Differ. 1997;8:589–598. [PubMed] [Google Scholar]
- [9]Szatrowski T, Nathan C. Cancer Res. 1991;51:794–798. [PubMed] [Google Scholar]
- [10]Bae Y S, Kang S W, Seo M S, Baines I C, Tekle E, Chock P B, Rhee S G. J Biol Chem. 1997;272:217–221. [PubMed] [Google Scholar]
- [15]Schulze-Osthoff K, Bakker A C, Vanhaesebroeck B, Beyaert R, Jacob W A, Fiers W. J Biol Chem. 1992;267:5317–5323. [PubMed] [Google Scholar]
- [21]Cohen G, Kim M, Ogwu V. J Neurosci Methods. 1996;67:53–56. [PubMed] [Google Scholar]
- [28]Yan T, Oberley L W, Zhong W, St. Clair D K. Cancer Res. 1996;56:2864–2871. [PubMed] [Google Scholar]
- [30]Fernandez-Pol J A, Hamilton P D, Klos D J. Cancer Res. 1982;42:609–617. [PubMed] [Google Scholar]
- [35]Natarajan V, Taher M M, Roehm B, Parinandi N L, Schmid H H O, Kiss Z, Garcia J G N. J Biol Chem. 1993;268:930–937. [PubMed] [Google Scholar]
- [45]Hainaut P, Milner J. Cancer Res. 1993;53:4469–4473. [PubMed] [Google Scholar]
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Yoshida, L. S., Nishida, S., Shimoyama, T., Kawahara, T., Kondo-Teshima, S., Rokutan, K., Kobayashi, T., & Tsunawaki, S. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.147 · Cited by 7 · see citing works
- Authors
- Arnold, R. S., Shi, J., Murad, E., Whalen, A. M., Sun, C. Q., Polavarapu, R., Parthasarathy, S., Petros, J. A., & Lambeth, J. D.
- Affiliations
- Emory University (US)
- ORCID
- Petros, John A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-05
- Volume
- 98
- Issue
- 10
- Pages
- 5550-5555
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC33250
- OpenAlex
- W2011993914
- Cited by
- 486
- References
- 50
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 10 · 2023: 12 · 2022: 10 · 2021: 14 · 2020: 15 · 2019: 14 · 2018: 8 · 2017: 24 · 2016: 17 · 2015: 20 · 2014: 11 · 2013: 19 · 2012: 19
- FWCI
- 10.36
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA-84138, R01CA084138)
- 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
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NOX1, hydrogen peroxide, reactive oxygen species, NADPH oxidase, cell transformation, cell growth, catalase, superoxide, tumorigenicity, gp91phox, cell cycle genes, gene expression, oxidative stress, NIH3T3 cells, cancer genes, athymic mice
- MeSH terms
- NADPH Oxidase 1, Animals, Base Sequence, Catalase, Cell Division, Cell Line, Cell Transformation, Neoplastic, Hydrogen Peroxide, Mice, Nude, NADH, NADPH Oxidoreductases, DNA Primers, Reverse Transcriptase Polymerase Chain Reaction, Mice
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