Cited by 519Immune Response and InflammationNF-κB Signaling PathwaysInflammasome and immune disorders

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Lipopolysaccharide-mediated Reactive Oxygen Species and Signal Transduction in the Regulation of Interleukin-1 Gene Expression

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Hsu, Hsien-Yeh, Wen, Meng-Hsuan·2002·Journal of Biological Chemistry

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Abstract

Lipopolysaccharide (LPS) stimulates macrophages to release inflammatory cytokines, interleukin-1 beta (IL-1), and tumor necrosis factor (TNF). LPS-induced TNF suppresses scavenger receptor functions in macrophages (van Lenten, B. J., and Fogelman, A. M. (1992) J. Immunol. 148, 112-116), which is regulated by TNF-mediated protein kinases (Hsu, H. Y., and Twu, Y. C. (2000) J. Biol. Chem. 275, 41035-41048). To examine the molecular mechanism for LPS induction of IL-1 in macrophages, we demonstrated that LPS quickly stimulated reactive oxygen species (ROS), and 3 h later induced prointerleukin-1 beta (pro-IL-1, precursor of IL-1) production and IL-1 secretion. LPS stimulated pro-IL-1 message/protein between 3 and 10 h; however, there was a 40% reduction of pro-IL-1 in preincubation of the antioxidant, N-acetylcysteine (NAC). Moreover, NAC moderated LPS-induced IL-1 secretion partially via interleukin 1-converting enzyme. The maximal activity of LPS-induced ERK, JNK, and p38 was 12- (30 min), 5- (30 min), and 16-fold (15 min), respectively. In contrast, NAC reduced ERK activity to 60% and decreased p38 activity to the basal level, but JNK activity was induced 2-fold. Furthermore, the pharmacological antagonists LY294002, SB203580, curcumin, calphostin C, and PD98059 revealed the diverse roles of LPS-mediated protein kinases in pro-IL-1. On the other hand, NAC and diphenyleneiodonium chloride partially inhibited LPS-induced Rac activity and protein-tyrosine kinase (PTK), indicating that LPS-mediated ROS and NADPH oxidase correspond to Rac activation and IL-1 expression. Our findings establish for the first time that LPS-mediated PTK/phosphatidylinositol 3-kinase/Rac/p38 pathways play a more important role than pathways of PTK/PKC/MEK/ERK and of PTK/phosphatidylinositol 3-kinase/Rac/JNK in the regulation of pro-IL-1/IL-1. The findings also further elucidate the critical role of LPS-mediated ROS in signal transduction pathways. Our results suggest that understanding LPS-transduced signals in IL-1 induction upon the antibacterial action of macrophages should provide a therapeutic strategy for aberrant inflammatory responses leading to severe cellular injury or concurrent multiorgan septic damage.

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Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF‐kappa B transcription factor and HIV‐1.
Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,793
A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266
A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
Han, J., Lee, J. D., Bibbs, L., & Ulevitch, R. J. (1994) · Science · doi:10.1126/science.7914033 · Cited by 2,647
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
The stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
The Regulation of AP-1 Activity by Mitogen-activated Protein Kinases
Karin, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16483 · Cited by 2,423
Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine
Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7420 · Cited by 2,244
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Gutkind, J. S. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,629
Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin
Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442
The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
Marais, R., Wynne, J., & Treisman, R. (1993) · Cell · doi:10.1016/0092-8674(93)90237-k · Cited by 1,275
Caspase-1 processes IFN-γ-inducing factor and regulates LPS-induced IFN- γ production
Ghayur, T., Banerjee, S., Hugunin, M., Butler, D., Herzog, L., Carter, A. B., Quintal, L. J., Sekut, L., Talanian, R. V., Paskind, M. P., et al. (1997) · Nature · doi:10.1038/386619a0 · Cited by 1,204
Molecular Cloning of the Interleukin-1β Converting Enzyme
Cerretti, D. P., Kozlosky, C. J., Mosley, B., Nelson, N. C., Ness, K. V., Greenstreet, T. A., March, C. J., Kronheim, S. R., Druck, T., Cannizzaro, L. A., et al. (1992) · Science · doi:10.1126/science.1373520 · Cited by 1,147
Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism
Wong, G. H. W., & Goeddel, D. V. (1988) · Science · doi:10.1126/science.3263703 · Cited by 914
Kappa B-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of the tumor necrosis factor alpha gene in primary macrophages
Shakhov, A. N., Collart, M. A., Vassalli, P., Nedospasov, S. A., & Jongeneel, C. V. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.1.35 · Cited by 819
Endotoxin signal transduction in macrophages
Sweet, M. J., & Hume, D. A. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.60.1.8 · Cited by 790
Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
Han, J., Jiang, Y., Li, Z., Kravchenko, V. V., & Ulevitch, R. J. (1997) · Nature · doi:10.1038/386296a0 · Cited by 766
Rho Family GTPases Regulate p38 Mitogen-activated Protein Kinase through the Downstream Mediator Pak1
Zhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., & Bokoch, G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23934 · Cited by 726
Cdc42 and PAK-mediated Signaling Leads to Jun Kinase and p38 Mitogen-activated Protein Kinase Activation
Bagrodia, S., Dérijard, B., Davis, R. J., & Cerione, R. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.27995 · Cited by 636
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
Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain
Binétruy, B., Smeal, T., & Karin, M. (1991) · Nature · doi:10.1038/351122a0 · Cited by 598
Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase
O’Donnell, V. B., Tew, D. G., Jones, O. T. G., & ENGLAND, P. J. (1993) · Biochemical Journal · doi:10.1042/bj2900041 · Cited by 588
Interleukin-1
Dinarello, C. A. (1997) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(97)00023-3 · Cited by 581
Involvement of Reactive Oxygen Species in Cytokine and Growth Factor Induction of c-fos Expression in Chondrocytes
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 530
ATF‐2 contains a phosphorylation‐dependent transcriptional activation domain.
Livingstone, C., Patel, G., & Jones, N. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07167.x · Cited by 494
LPS-binding proteins and receptors
Fenton, M. J., & Golenbock, D. T. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.64.1.25 · Cited by 474
Activation of c-Jun N-terminal kinase in bacterial lipopolysaccharide-stimulated macrophages.
Hambleton, J., Weinstein, S. L., Lem, L., & DeFranco, A. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2774 · Cited by 471
Bacterial modulins: a novel class of virulence factors which cause host tissue pathology by inducing cytokine synthesis
Henderson, B. E., Poole, S., & Wilson, M. (1996) · Microbiological Reviews · doi:10.1128/mr.60.2.316-341.1996 · Cited by 412
Lipopolysaccharide Induces Rac1-dependent Reactive Oxygen Species Formation and Coordinates Tumor Necrosis Factor-α Secretion through IKK Regulation of NF-κB
Sanlioglu, S., Williams, C. M., Samavati, L., Butler, N. S., Wang, G., McCray, P. B., Ritchie, T. C., Hunninghake, G. W., Zandi, E., & Engelhardt, J. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102061200 · Cited by 395
Proliferating or interleukin 1-activated human vascular smooth muscle cells secrete copious interleukin 6.
Loppnow, H., & Libby, P. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114498 · Cited by 378
The Lipopolysaccharide-activated Toll-like Receptor (TLR)-4 Induces Synthesis of the Closely Related Receptor TLR-2 in Adipocytes
Lin, Y., Lee, H., Berg, A. H., Lisanti, M. P., Shapiro, L. S., & Scherer, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002137200 · Cited by 360
Rapid and Preferential Activation of the c- jun Gene during the Mammalian UV Response
Devary, Y., Gottlieb, R. A., Lau, L. F., & Karin, M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2804 · Cited by 344
LPS induces apoptosis in macrophages mostly through the autocrine production of TNF-α
Xaus, J., Comalada, M., Valledor, A. F., Lloberas, J., López-Soriano, F., Argilés, J. M., Bogdan, C., & Celada, A. (2000) · Blood · doi:10.1182/blood.v95.12.3823 · Cited by 331
Neutrophils exposed to bacterial lipopolysaccharide upregulate NADPH oxidase assembly.
DeLeo, F. R., Renee, J., McCormick, S. J., Nakamura, M., Apicella, M. A., Weiss, J. P., & Nauseef, W. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci949 · Cited by 312
Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages.
Weinstein, S. L., Gold, M. R., & DeFranco, A. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4148 · Cited by 311
Molecular mechanisms of endotoxin activity
Schletter, J., Heine, H., Ulmer, A. J., & Rietschel, E. T. (1995) · Archives of Microbiology · doi:10.1007/bf02529735 · Cited by 308
Both Erk and p38 Kinases Are Necessary for Cytokine Gene Transcription
Carter, A. B., Monick, M. M., & Hunninghake, G. W. (1999) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.20.4.3420 · Cited by 305
Cellular Events Mediated by Lipopolysaccharide-stimulated Toll-like Receptor 4
Yang, H., Young, D. W., Gusovsky, F., & Chow, J. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002896200 · Cited by 267
The stress-activated protein kinases are major c-Jun amino-terminal kinases activated by ischemia and reperfusion
Pombo, C. M., Bonventre, J. V., Avruch, J., Woodgett, J. R., Kyriakis, J. M., & Force, T. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47229-8 · Cited by 259
Inhibition of MAP Kinase Kinase Prevents Cytokine and Prostaglandin E2 Production in Lipopolysaccharide-Stimulated Monocytes
Scherle, P., Jones, E. A., Favata, M. F., Daulerio, A. J., Covington, M. B., Nurnberg, S., Magolda, R. L., & Trzăskos, J. M. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.10.5681 · Cited by 256
Signal transduction by reactive oxygen species in non-phagocytic cells
Finkel, T. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.65.3.337 · Cited by 256
Expression of mitogen-inducible cyclooxygenase induced by lipopolysaccharide
Hwang, D. H., Jang, B. C., Yu, G., & Boudreau, M. D. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00154-8 · Cited by 248
The Ras-JNK Pathway Is Involved in Shear-Induced Gene Expression
Li, Y.-S. J., Shyy, J. Y.-J., Li, S., Lee, J., Su, B., Karin, M., & Chien, S. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.5947 · Cited by 230
Lipopolysaccharide Signals Activation of Tumor Necrosis Factor Biosynthesis Through the Ras/Raf-1/MEK/MAPK Pathway
Geppert, T. D., Whitehurst, C. E., Thompson, P., & Beutler, B. (1994) · Molecular Medicine · doi:10.1007/bf03403535 · Cited by 228
An automated micro-fluorometric assay for monitoring oxidative burst activity of phagocytes
Wan, C. P., Myung, E., & Lau, B. H. S. (1993) · Journal of Immunological Methods · doi:10.1016/0022-1759(93)90150-6 · Cited by 218
Activation of the mitogen-activated protein kinase signaling pathway in neutrophils. Role of oxidants.
Fialkow, L., Chan, C. K., Rotin, D., Grinstein, S., & Downey, G. P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47414-5 · Cited by 212
Selective activation of the mitogen-activated protein kinase subgroups c-Jun NH2 terminal kinase and p38 by IL-1 and TNF in human articular chondrocytes.
Geng, Y., Valbracht, J., & Lotz, M. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119056 · Cited by 211
c-Jun N-Terminal Phosphorylation Correlates with Activation of the JNK Subgroup but Not the ERK Subgroup of Mitogen-Activated Protein Kinases
Minden, A., Lin, A., Smeal, T., Dérijard, B., Cobb, M., Davis, R., & Karin, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6683 · Cited by 195
Ligands of Macrophage Scavenger Receptor Induce Cytokine Expression via Differential Modulation of Protein Kinase Signaling Pathways
Hsu, H., Chiu, S.-L., Wen, M., Chen, K.-Y., & Hua, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011117200 · Cited by 169
Self-citation
Lipopolysaccharide Activates Caspase-1 (Interleukin-1–Converting Enzyme) in Cultured Monocytic and Endothelial Cells
Schumann, R. R., Belka, C., Reuter, D., Lamping, N., Kirschning, C. J., Weber, J. R., & Pfeil, D. (1998) · Blood · doi:10.1182/blood.v91.2.577 · Cited by 165
Toll-like receptors: how they work and what they do
Beutler, B. (2002) · Current opinion in hematology · doi:10.1097/00062752-200201000-00002 · Cited by 153
Expression of Toll-Like Receptor 2 on γδ T Cells Bearing Invariant Vγ6/Vδ1 Induced by Escherichia coli Infection in Mice
Mokuno, Y., Matsuguchi, T., Takano, M., Nishimura, H., Washizu, J., Ogawa, T., Takeuchi, O., Akira, S., Nimura, Y., & Yoshikai, Y. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.931 · Cited by 148
Lipopolysaccharide induces activation of the Raf-1/MAP kinase pathway. A putative role for Raf-1 in the induction of the IL-1 beta and the TNF- alpha genes.
Reimann, T., Büscher, D., Hipskind, R. A., Krautwald, S., Lohmann-Matthes, M.-L., & Baccarini, M. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.12.5740 · Cited by 146
Evaluation of the role of mitogen-activated protein kinases in the expression of inducible nitric oxide synthase by IFN-gamma and TNF-alpha in mouse macrophages.
Chan, E. D., Winston, B. W., Uh, S., Wynes, M. W., Rose, D. M., & Riches, D. W. H. (1999) · PubMed · Cited by 139
Metabolic Impairment Induces Oxidative Stress, Compromises Inflammatory Responses, and Inactivates a Key Mitochondrial Enzyme in Microglia
Park, L. C. H., Zhang, H., Sheu, K. R., Calingasan, N. Y., Kristal, B. S., LINDSAY, J. G., & Gibson, G. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721948.x · Cited by 139
Evaluation of the Role of Mitogen-Activated Protein Kinases in the Expression of Inducible Nitric Oxide Synthase by IFN-γ and TNF-α in Mouse Macrophages
Chan, E. D., Winston, B. W., Uh, S., Wynes, M. W., Rose, D. M., & Riches, D. W. H. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.1.415 · Cited by 125
Regulation of the phagocyte respiratory burst by small GTP-binding proteins
Bokoch, G. (1995) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)88960-6 · Cited by 124
Regulation of TNF Expression by Multiple Mitogen-Activated Protein Kinase Pathways
Zhu, W. P., Downey, J. S., Gu, J., Padova, F. D., Gram, H., & Han, J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.12.6349 · Cited by 120
Lipopolysaccharide-induced inhibition of scavenger receptor expression in human monocyte-macrophages is mediated through tumor necrosis factor-alpha
Lenten, B. J. V., & Fogelman, A. M. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.1.112 · Cited by 116
Electron Leakage from the Mitochondrial NADPH-Adrenodoxin Reductase-Adrenodoxin-P450scc (Cholesterol Side Chain Cleavage) System
Hanukoglu, I., Rapoport, R., Weiner, L. M., & Sklan, D. J. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1452 · Cited by 116
Lipopolysaccharide Inhibits TNF-Induced Apoptosis: Role of Nuclear Factor-κB Activation and Reactive Oxygen Intermediates
Manna, S. K., & Aggarwal, B. B. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.3.1510 · Cited by 104
Ligand Binding to Macrophage Scavenger Receptor-A Induces Urokinase-type Plasminogen Activator Expression by a Protein Kinase-dependent Signaling Pathway
Hsu, H., Hajjar, D. P., Khan, K. M. F., & Falcone, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.1240 · Cited by 99
Self-citation
Lipopolysaccharide inhibits TNF-induced apoptosis: role of nuclear factor-kappaB activation and reactive oxygen intermediates.
Manna, S. K., & Aggarwal, B. B. (1999) · PubMed · Cited by 86
A CRE/ATF-Like Site in the Upstream Regulatory Sequence of the Human Interleukin 1β Gene Is Necessary for Induction in U937 and THP-1 Monocytic Cell Lines
Gray, J. G., Chandra, G., Clay, W. C., Stinnett, S. W., Haneline, S. A., Lorenz, J. J., Patel, I. R., Wisely, G. B., Furdon, P. J., Taylor, J. D., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.6678-6689.1993 · Cited by 85
Glutathione Levels Determine Apoptosis in Macrophages
Boggs, S. E., McCormick, T. S., & Lapetina, E. G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8765 · Cited by 78
Impaired Pulmonary NF-κB Activation in Response to Lipopolysaccharide in NADPH Oxidase-Deficient Mice
Koay, M. A., Christman, J. W., Segal, B. H., Venkatakrishnan, A., Blackwell, T. R., Holland, S. M., & Blackwell, T. S. (2001) · Infection and Immunity · doi:10.1128/iai.69.10.5991-5996.2001 · Cited by 77
Hydrogen peroxide-mediated transcriptional induction of macrophage colony-stimulating factor by TGF-beta1
Hong, Y. H., Peng, H., Fata, V. L., & Liao, J. K. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.5.2418 · Cited by 77
Tumor Necrosis Factor-α-mediated Protein Kinases in Regulation of Scavenger Receptor and Foam Cell Formation on Macrophage
Hsu, H., & Twu, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003464200 · Cited by 57
Self-citation
Role of Protein Kinase C in Basal and Hydrogen Peroxide-Stimulated NF-κB Activation in the Murine Macrophage J774A.1 Cell Line
Kaul, N., Gopalakrishna, R., Gundimeda, U., Choi, J., & Forman, H. J. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0487 · Cited by 54
The interleukin-1 and interleukin-1 converting enzyme families in the cardiovascular system.
Loppnow, H., Werdan, K., Reuter, G., & Flad, H.-D. (1998) · PubMed · Cited by 45
Escherichia coli-induced activation of neutrophil NADPH-oxidase: lipopolysaccharide and formylated peptides act synergistically to induce release of reactive oxygen metabolites
Karlsson, A., Markfjall, M., Strömberg, N., & Dahlgren, C. (1995) · Infection and Immunity · doi:10.1128/iai.63.12.4606-4612.1995 · Cited by 29
Antioxidant enzymes in xeroderma pigmentosum fibroblasts.
Crawford, D. R., Zbinden, I., Moret, R., & Cerutti, P. (1988) · PubMed · Cited by 21
Scavenger Receptors May Regulate Nitric Oxide Production from Macrophages Stimulated by LPS
Matsuno, R., Aramaki, Y., Arima, H., & Tsuchiya, S. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7195 · Cited by 20

Research works printed but not linked: 6

Gray, 1993, Mol. Cell. Biol., 13, 6678
Loppnow, 1998, Eur. Cytokine Netw., 9, 675
Devary, 1991, Mol. Cell. Biol., 11, 2804
Crawford, 1988, Cancer Res., 48, 2132
Minden, 1994, Mol. Cell. Biol., 14, 6683
Wong, 1996, Exs (Basel), 77, 321

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Authors: Hsu, H.-Y., & Wen, M.-H.
Affiliations: National Yang Ming University (TW)
Corresponding author: Hsu, Hsien-Yeh
ORCID: Wen, Meng-Hsuan
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-06
Volume: 277
Issue: 25
Pages: 22131-22139
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m111883200
OpenAlex: W2016146035
Cited by: 519
References: 72
Citations by year: 2026: 13 · 2025: 17 · 2024: 20 · 2023: 21 · 2022: 21 · 2021: 27 · 2020: 22 · 2019: 23 · 2018: 25 · 2017: 33 · 2016: 27 · 2015: 21 · 2014: 18 · 2013: 19 · 2012: 14
FWCI: 7.22
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6719 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Keywords: lipopolysaccharide, IL-1β, reactive oxygen species, N-acetylcysteine, macrophages, Rac, p38 MAPK, JNK, ERK, phosphatidylinositol 3-kinase, tyrosine kinase, NADPH oxidase, signal transduction, inflammatory cytokines, TNF-α
MeSH terms: Animals, Carrier Proteins, Cell Line, Chromones, Curcumin, Enzyme Activation, Enzyme Inhibitors, Enzyme-Linked Immunosorbent Assay, Flavonoids, Gene Expression Regulation, Genes, Dominant, Imidazoles, Interleukin-1, Lipopolysaccharides, Macrophages, Models, Biological, Morpholines, Naphthalenes, Oxygen, Protein Binding, Pyridines, Time Factors, Transfection, Signal Transduction, Reactive Oxygen Species, rac1 GTP-Binding Protein, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 4, Mice

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Lipopolysaccharide-mediated Reactive Oxygen Species and Signal Transduction in the Regulation of Interleukin-1 Gene Expression

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