Cited by 892Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

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Reactive Oxygen Species and Cell Signaling: Respiratory Burst in Macrophage Signaling

Forman, Henry Jay, Torres, Martine·2002·American Journal of Respiratory and Critical Care Medicine

DOI 10.1164/rccm.2206007

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Abstract

Phagocytes such as neutrophils and macrophages produce reactive oxygen species (ROS) during phagocytosis or stimulation with a wide variety of agents through activation of nicotinamide adenine dinucleotide phosphate reduced (NADPH) oxidase that is assembled at the plasma membrane from resident plasma membrane and cytosolic protein components. One of the subunits of the phagocyte NADPH oxidase is now recognized as a member of a family of NADPH oxidases, or NOX, present in cells other than phagocytes. Physiologic generation of ROS has been implicated in a variety of physiologic responses from transcriptional activation to cell proliferation and apoptosis. The increase in superoxide and hydrogen peroxide (H2O2) that results from stimulation of the NADPH oxidase is transient, in part due to the presence of the antioxidant enzymes, which return their concentrations to the prestimulation steady state level. Thus, the antioxidant enzymes may function in the “turn-off” phase of signal transduction by ROS. During its transient elevation, H2O2 may act as a modifier of key signaling enzymes through reversible oxidation of critical thiols. The rapid reaction of thiols with H2O2 when in their unprotonated state would provide a potential mechanism for the specificity that is necessary for physiologic cell signaling.

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Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
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Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961
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Thannickal, V. J., & Fanburg, B. L. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.6.l1005 · Cited by 2,950
Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
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
Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions
Pearson, G. (2001) · Endocrine Reviews · doi:10.1210/er.22.2.153 · Cited by 1,406
Oxidants as Stimulators of Signal Transduction
Suzuki, Y. J., Forman, H. J., & Sevanian, A. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00275-4 · Cited by 1,370
Self-citation
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Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040
Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
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
Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945
An essential role for free radicals and derived species in signal transduction
Lander, H. M. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.2.9039953 · Cited by 908
Oxidant Signaling in Vascular Cell Growth, Death, and Survival
Irani, K. (2000) · Circulation Research · doi:10.1161/01.res.87.3.179 · Cited by 756
Identification and characterization of Ref‐1, a nuclear protein that facilitates AP‐1 DNA‐binding activity.
Xanthoudakis, S., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05097.x · Cited by 708
Redox signaling: hydrogen peroxide as intracellular messenger
Rhee, S. G. (1999) · Experimental & Molecular Medicine · doi:10.1038/emm.1999.9 · Cited by 701
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Adler, V., Yin, Z., Tew, K. D., & Ronai, Z. A. (1999) · Oncogene · doi:10.1038/sj.onc.1203128 · Cited by 699
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Aikawa, R., Komuro, I., Yamazaki, T., Zou, Y., Kudoh, S., Tanaka, M. H., Shiojima, I., Hiroi, Y., & Yazaki, Y. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119709 · Cited by 687
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Janssen-Heininger, Y. M. W., Poynter, M. E., & Baeuerle, P. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00218-5 · Cited by 666
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Liu, Y., Guyton, K. Z., Gorospe, M., Xu, Q., Kokkonen, G. C., Mock, Y. D., Roth, G. S., & Holbrook, N. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.7.3604 · Cited by 350
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Gordon, S. B., & Read, R. C. (2002) · British Medical Bulletin · doi:10.1093/bmb/61.1.45 · Cited by 247
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Gao, X.-P., Standiford, T. J., Rahman, A., Newstead, M. W., Holland, S. M., Dinauer, M. C., Liu, Q.-H., & Malik, A. B. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.8.3974 · Cited by 177
A family of novel peroxidases, peroxiredoxins
Rhee, S. G., Kang, S. W., Netto, L. E. S., Seo, M. S., & Stadtman, E. R. (1999) · BioFactors · doi:10.1002/biof.5520100218 · Cited by 170
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Gow, A. J., & Ischiropoulos, H. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1085 · Cited by 163
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Koay, M. A., Gao, X., Washington, M. K., Parman, K. S., Sadikot, R. T., Blackwell, T. S., & Christman, J. W. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.5.4748 · Cited by 124
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Abe, M. K., Kartha, S., Karpova, A. Y., Li, J., Liu, P. T., Kuo, W.-L., & Hershenson, M. B. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.18.4.2958 · Cited by 119
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Rose, M., Rusyn, I., Bojes, H. K., Belyea, J., Cattley, R. C., & Thurman, R. G. (2000) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(99)00235-3 · Cited by 62
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Jihee Lee Kang, E. W. (2000) · Journal of Toxicology and Environmental Health · doi:10.1080/009841000156574 · Cited by 59
Evaluation of the process for superoxide production by NADPH oxidase in human neutrophils: evidence for cytoplasmic origin of superoxide
Kobayashi, T., Tsunawaki, S., & Seguchi, H. (2001) · Redox Report · doi:10.1179/135100001101536003 · Cited by 56
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Rojanasakul, Y., Ye, J., Chen, F., Wang, L., Cheng, N., Castranova, V., Vallyathan, V., & Shi, X. (1999) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007051402840 · Cited by 53
Hyperoxia upregulates the NO pathway in alveolar macrophages in vitro: role of AP-1 and NF-κB
Pepperl, S., Dörger, M., Ringel, F. A., Kupatt, C., & Krombach, F. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.280.5.l905 · Cited by 49
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Adhesion and Pollution Particle–Induced Oxidant Generation Is neither Necessary nor Sufficient for Cytokine Induction in Human Alveolar Macrophages
Mondal, K., Haskill, J. S., & Becker, S. (2000) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.22.2.3661 · Cited by 21
ADP stimulates the respiratory burst without activation of ERK and AKT in rat alveolar macrophages
Gozal, E., Forman, H. J., & Torrès, M. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00630-x · Cited by 18
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2000, Mutat Res, 448, 179
2001, Endocr Rev, 22, 153
1996, J Biol Chem, 271, 4138, 10.1074/jbc.271.8.4138 · DOI
1996, Int J Pediatr Hematol Oncol, 3, 387

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Authors: Forman, H. J., & Torres, M.
Affiliations: University of Southern California (US)
Department of Environmental Health Sciences, School of Public Health, University of Alabama at Birmingham, Birmingham, Alabama; and Department of Pediatrics, Children's Hospital Los Angeles Research Institute, Keck School of Medicine, University of Southern California, Los Angeles, California
ORCID: Forman, Henry Jay
Venue: American Journal of Respiratory and Critical Care Medicine
Publisher: Oxford University Press (OUP)
Published: 2002-12
Volume: 166
Issue: Supplement_1
Pages: S4-S8
ISSN: 1073-449X (ISSN-L)
1535-4970
DOI: 10.1164/rccm.2206007
OpenAlex: W1874751834
Cited by: 891
References: 67
Citations by year: 2026: 18 · 2025: 21 · 2024: 23 · 2023: 32 · 2022: 47 · 2021: 44 · 2020: 36 · 2019: 31 · 2018: 44 · 2017: 43 · 2016: 50 · 2015: 43 · 2014: 48 · 2013: 45 · 2012: 44
FWCI: 2.28
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: American Journal of Respiratory and Critical Care Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (R01HL037556, HL 37556)
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 (medical) › Nitric Oxide and Endothelin Effects
Keywords: reactive oxygen species, NADPH oxidase, respiratory burst, macrophages, signal transduction, hydrogen peroxide, superoxide, antioxidant enzymes, thioredoxin reductase, thioredoxin, redox signaling, phagocytes
MeSH terms: Humans, Hydrogen Peroxide, Macrophages, Oxidation-Reduction, Signal Transduction, Respiratory Burst, Protein Tyrosine Phosphatases, Reactive Oxygen Species, Mitogen-Activated Protein Kinases

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Reactive Oxygen Species and Cell Signaling: Respiratory Burst in Macrophage Signaling

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