The DOI matches its Crossref record; 42 of the 43 references it cites were found in a registry or an index.
Role of Neutrophil NADPH Oxidase in the Mechanism of Tumor Necrosis Factor-α-induced NF-κB Activation and Intercellular Adhesion Molecule-1 Expression in Endothelial Cells
Open accessAbstract
In this study, we explored a novel function of polymorphonuclear neutrophils (PMN) NAD(P)H oxidase in the mechanism of tumor necrosis factor-alpha (TNFalpha)-induced NF-kappaB activation and intercellular adhesion molecule-1 (ICAM-1) expression in endothelial cells. Studies were made in mice lacking the p47(phox) subunit of NAD(P)H oxidase as well as in cultured mouse lung vascular endothelial cells (MLVEC) from these mice. In response to TNFalpha challenge, NF-kappaB activation and ICAM-1 expression were significantly attenuated in lungs of p47(phox)(-/-) mice as compared with wild-type (WT) mice. The attenuated NF-kappaB activation in p47(phox)(-/-) mice was secondary to inhibition of NIK activity and subsequent IkappaBalpha degradation. Induction of neutropenia using anti-PMN serum prevented the initial TNFalpha-induced NF-kappaB activation and ICAM-1 expression in WT mice, indicating the involvement of PMN NAD(P)H oxidase in signaling these responses. Moreover, the responses were restored upon repletion with PMN obtained from WT mice but not with PMN from p47(phox)(-/-) mice. These findings were recapitulated in MLVEC co-cultured with PMN, suggesting that NF-kappaB activation and resultant ICAM-1 expression in endothelial cells occurred secondary to oxidants generated by the PMN NAD(P)H oxidase complex. The functional relevance of the PMN NAD(P)H oxidase in mediating TNFalpha-induced ICAM-1-dependent endothelial adhesivity was evident by markedly reduced adhesion of p47(phox)(-/-) PMN in co-culture experiments. Thus, oxidant signaling by the PMN NAD(P)H oxidase complex is an important determinant of TNFalpha-induced NF-kappaB activation and ICAM-1 expression in endothelial cells.
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“A large number of cytokines and hormones have been shown to induce NOX2 expression, including angiotensin II (658, 714, 802), thrombin (725), and TNF-α (275, 964).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [275]
Citations
Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Function and Activation of NF-kappaB in the Immune System
Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745
Leukocyte-endothelial adhesion molecules
Carlos, T., & Harlan, J. (1994) · Blood · doi:10.1182/blood.v84.7.2068.bloodjournal8472068 · Cited by 2,687
Oxidative stress as a mediator of apoptosis
Buttke, T. M., & Sandstrom, P. A. (1994) · Immunology Today · doi:10.1016/0167-5699(94)90018-3 · Cited by 2,149
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147
Hsu, H., Shu, H., Pan, M., & Goeddel, D. V. (1996) · Cell · doi:10.1016/s0092-8674(00)80984-8 · Cited by 1,998
Liu, Z.-G., Hsu, H., Goeddel, D. V., & Karin, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81375-6 · Cited by 1,937
Schreck, R., Albermann, K., & Baeuerle, P. A. (1992) · Free Radical Research Communications · doi:10.3109/10715769209079515 · Cited by 1,388
MAP3K-related kinase involved in NF-KB induction by TNF, CD95 and IL-1
Malinin, N. L., Boldin, M., Kovalenko, A. V., & Wallach, D. (1997) · Nature · doi:10.1038/385540a0 · Cited by 1,279
TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182
Signal transduction through NF-κB
May, M. J., & Ghosh, S. (1998) · Immunology Today · doi:10.1016/s0167-5699(97)01197-3 · Cited by 1,098
Dustin, M. L., & Springer, T. A. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.1.321 · Cited by 985
Pollock, J. D., Williams, D. A., Gifford, M. A. C., Li, L. L., Du, X., Fisherman, J., Orkin, S. H., Doerschuk, C. M., & Dinauer, M. C. (1995) · Nature Genetics · doi:10.1038/ng0295-202 · Cited by 921
Manna, S. K., Mukhopadhyay, A., & Aggarwal, B. B. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.12.6509 · Cited by 876
Oxidative stress and nuclear factor-κB activation
Bowie, A., & O'Neill, L. A. J. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00296-8 · Cited by 860
Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 836
Diamond, M., Staunton, D. E., Marlin, S. D., & Springer, T. A. (1991) · Cell · doi:10.1016/0092-8674(91)90548-d · Cited by 778
Intercellular adhesion molecule-1 (ICAM-1) expression and cell signaling cascades
Hubbard, A. K., & Rothlein, R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00223-9 · Cited by 594
NF-kappa B as a frequent target for immunosuppressive and anti-inflammatory molecules.
Baeuerle, P. A., & Baichwal, V. R. (1997) · PubMed · Cited by 573
Ledebur, H. C., & Parks, T. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.933 · Cited by 536
Baeuerle, P. A., & Baichwal, V. R. (1997) · Advances in immunology · doi:10.1016/s0065-2776(08)60742-7 · Cited by 516
NADPH oxidase–derived free radicals are key oxidants in alcohol-induced liver disease
Kono, H., Rusyn, I., Yin, M., Gäbele, E., Yamashina, S., Dikalova, A., Kadiiska, M. B., Connor, H. D., Mason, R. P., Segal, B. H., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9020 · Cited by 493
Hayashi, T., Ueno, Y., & Okamoto, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82135-4 · Cited by 485
The p47phox mouse knock-out model of chronic granulomatous disease.
Jackson, S. H., Gallin, J. I., & Holland, S. M. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.3.751 · Cited by 484
Oxidation-Reduction and the Molecular Mechanism of a Regulatory RNA-Protein Interaction
Hentze, M. W., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1989) · Science · doi:10.1126/science.2711187 · Cited by 377
A one-hour minipreparation technique for extraction of DNA-binding proteins from animal tissues.
Deryckère, F., & Gannon, F. (1994) · PubMed · Cited by 329
Satriano, J. A., Shuldiner, M., Hora, K., Xing, Y., Shan, Z., & Schlöndorff, D. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116737 · Cited by 274
Hou, J., Baichwal, V. R., & Cao, Z. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.24.11641 · Cited by 217
Korn, S. H., Wouters, E. F. �., Vos, N., & Janssen-Heininger, Y. M. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104321200 · Cited by 204
Yoshida, M., Korfhagen, T. R., & Whitsett, J. A. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7514 · Cited by 162
Krunkosky, T. M., Fischer, B. M., Martin, L. D., Jones, N., Akley, N. J., & Adler, K. B. (2000) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.22.6.3925 · Cited by 145
Peng, Q., Wei, Z., & Lau, B. H. S. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050045 · Cited by 95
Rahman, A., Bando, M., Kefer, J., Anwar, K. N., & Malik, A. B. (1999) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12184-0 · Cited by 74
Self-citationDusi, S., Bianca, V. D., Donini, M., Nadalini, K. A., & Rossi, F. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.10.4615 · Cited by 69
NADPH oxidase subunits and superoxide production in porcine pulmonary artery endothelial cells
Höhler, B., Holzapfel, B., & Kummer, W. (2000) · Histochemistry and Cell Biology · doi:10.1007/s004180000160 · Cited by 58
Takeuchi, J. S., Hirota, K., Itoh, T., Shinkura, R., Kitada, K., Yodoi, J., Namba, T., & Fukuda, K. (2000) · Antioxidants and Redox Signaling · doi:10.1089/ars.2000.2.1-83 · Cited by 52
Lo, T.-M., & Thayer, S. A. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.264.3.c641 · Cited by 40
Paxton, L. L. L., Li, L.-J., Secor, V. H., Duff, J. L., Naik, S. M., Shibagaki, N., & Caughman, S. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15928 · Cited by 38
Balazovich, K. J., Suchard, S. J., Remick, D. G., & Boxer, L. (1996) · Blood · doi:10.1182/blood.v88.2.690.bloodjournal882690 · Cited by 30
The separation of the granulocytes from different rat strains A comparative study
Szűcs, S., Varga, C., Ember, I., & Kertai, P. (1994) · Journal of Immunological Methods · doi:10.1016/0022-1759(94)90093-0 · Cited by 24
Schumann, M. A., Leung, C. C., & Raffin, T. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13124 · Cited by 14
Research works printed but not linked: 5
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Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897
Self-citationRole of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,651
Incalza, M. A., D’Oria, R., Natalicchio, A., Perrini, S., Laviola, L., & Giorgino, F. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.05.005 · Cited by 1,419
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology
Li, J.-M., & Shah, A. M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00124.2004 · Cited by 773
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Metadata
- Authors
- Fan, J., Frey, R. S., Rahman, A., & Malik, A. B.
- Affiliations
- University of Illinois Chicago (US)
- Corresponding author
- Fan, Jie
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 277
- Issue
- 5
- Pages
- 3404-3411
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1966454841
- Cited by
- 130
- References
- 43
- Citations by year
- 2026: 1 · 2024: 4 · 2022: 1 · 2021: 6 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 5
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (T32 HL-07829, P01HL060678, HL-45638, HL 27016, HL 60678, R01HL045638, T32HL007829)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- neutrophil NADPH oxidase, p47phox, TNF-α, NF-κB activation, ICAM-1 expression, endothelial cells, NIK, IκBα degradation, neutrophils, oxidant signaling, neutrophil-endothelial cell adhesion, neutropenia
- MeSH terms
- NF-KappaB Inhibitor alpha, Animals, DNA-Binding Proteins, Endothelium, Vascular, Gene Expression Regulation, Lung, Mice, Inbred C57BL, Models, Biological, Neutrophils, Nuclear Proteins, Phosphoproteins, Pulmonary Circulation, Tumor Necrosis Factor-alpha, Blotting, Northern, NF-kappa B, Mice, Knockout, Intercellular Adhesion Molecule-1, NADPH Oxidases, I-kappa B Proteins, Mice
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