Lipopolysaccharide-mediated Reactive Oxygen Species and Signal Transduction in the Regulation of Interleukin-1 Gene Expression
Open accessAbstract
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.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the NF-κB system, NF-κB is normally held inactive in the cytoplasm by binding to an inhibitor IκB; pro-inflammatory cytokines such as TNF-α, LPS and IL-1 act by binding to receptors at the cell surface and initiating signalling pathways that lead to activation of IKK; IKK phosphorylates IκB causing its release and degradation, allowing NF-κB to translocate to the nucleus where it can activate a
“In the NF-κB system (e.g. [2020-2024]) (Fig 8), NF-κB is normally held inactive in the cytoplasm by binding to an inhibitor IκB (often IκBα). Pro-inflammatory cytokines such as TNF-α, LPS [2025-2030] and IL-1 [2031] act by binding to receptors at the cell surface and initiating signalling pathways that lead to the activation of a particular kinase, IκB kinase or IKK. This kinase phosphorylates the”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [2027]
Cites
Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,816 · see citing works
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 · see citing works
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N., Bull, H., Calaycay, J., Chapman, K., Howard, A., Kostura, M., Miller, D. K., Molineaux, S., Weidner, J., Auniņš, J., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,725 · see citing works
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 · see citing works
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 · see citing works
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 2,409 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 795 · see citing works
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 · see citing works
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 · see citing works
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 667 · see citing works
Bagrodia, S., Dérijard, B., Davis, R. J., & Cerione, R. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.27995 · Cited by 635 · 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
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 · see citing works
O’Donnell, V. B., Tew, D. G., Jones, O. T. G., & ENGLAND, P. J. (1993) · Biochemical Journal · doi:10.1042/bj2900041 · Cited by 588 · see citing works
Dinarello, C. A. (1997) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(97)00023-3 · Cited by 581 · see citing works
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 530 · see citing works
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 · see citing works
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 480 · see citing works
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 · see citing works
Minden, A., Lin, A., Smeal, T., Dérijard, B., Cobb, M. H., Davis, R. J., & Karin, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6683 · Cited by 467 · see citing works
Henderson, B. E., Poole, S., & Wilson, M. (1996) · Microbiological Reviews · doi:10.1128/mr.60.2.316-341.1996 · Cited by 419 · see citing works
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 · see citing works
Loppnow, H., & Libby, P. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114498 · Cited by 378 · see citing works
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 355 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 269 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Geppert, T. D., Whitehurst, C. E., Thompson, P., & Beutler, B. (1994) · Molecular Medicine · doi:10.1007/bf03403535 · Cited by 228 · see citing works
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 · see citing works
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 · see citing works
Geng, Y., Valbracht, J., & Lotz, M. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119056 · Cited by 211 · see citing works
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 · see citing works
Self-citationSchumann, 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Chan, E. D., Winston, B. W., Uh, S., Wynes, M. W., Rose, D. M., & Riches, D. W. H. (1999) · PubMed · Cited by 139 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Lenten, B. J. V., & Fogelman, A. M. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.1.112 · Cited by 116 · see citing works
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 · see citing works
Manna, S. K., & Aggarwal, B. B. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.3.1510 · Cited by 103 · see citing works
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 · see citing works
Self-citationManna, S. K., & Aggarwal, B. B. (1999) · PubMed · Cited by 86 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 74 · see citing works
Hsu, H., & Twu, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003464200 · Cited by 57 · see citing works
Self-citationKaul, 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 · see citing works
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 · see citing works
Karlsson, A., Markfjall, M., Strömberg, N., & Dahlgren, C. (1995) · Infection and Immunity · doi:10.1128/iai.63.12.4606-4612.1995 · Cited by 29 · see citing works
Antioxidant enzymes in xeroderma pigmentosum fibroblasts.
Crawford, D. R., Zbinden, I., Moret, R., & Cerutti, P. (1988) · PubMed · Cited by 21 · see citing works
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 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Liu, B., & Hong, J.-S. (2003) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.035048 · Cited by 1,095 · see citing works
“Furthermore, studies on LPS-stimulated macrophages have demonstrated that generation of ROS is an upstream event serving to regulate the production of other proinflammatory factors such as TNF and IL-1 (Sanlioglu et al., 2001; Hsu and Wen, 2002).”
BackgroundInterleukin-1 and neuronal injury
Allan, S. M., Tyrrell, P. J., & Rothwell, N. J. (2005) · Nature Reviews Immunology · doi:10.1038/nri1664 · Cited by 992 · see citing works
“Expression of the genes that encode IL-1α and IL-1β is induced by various pro-inflammatory stimuli (including bacterial and viral products), other cytokines (notably TNF), and cellular injury and hypoxi”
BackgroundA review of the interaction among dietary antioxidants and reactive oxygen species
Seifried, H. E., Anderson, D. E., Fisher, E. I., & Milner, J. A. (2007) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2006.10.007 · Cited by 895 · see citing works
“Hsu and Wen [43] demonstrated that IL1h production by LPS-stimulated macrophages requires ROS; preincubation with the antioxidant N-acetylcysteine decreased IL1h levels by 40%.”
BackgroundMatsuzawa, A., Saegusa, K., Noguchi, T., Sadamitsu, C., Nishitoh, H., Nagai, S., Koyasu, S., Matsumoto, K., Takeda, K., & Ichijo, H. (2005) · Nature Immunology · doi:10.1038/ni1200 · Cited by 667 · see citing works
“Along with published data showing that p38 inhibitor blocks LPS-induced production of IL-6, TNF and IL-1&beta”
BackgroundBegum, A. N., Jones, M. R., Lim, G. P., Morihara, T., Kim, P., Heath, D. D., Rock, C. L., Pruitt, M. A., Yang, F., Hudspeth, B., et al. (2008) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.137455 · Cited by 604 · see citing works
Qin, L., Liu, Y., Wang, T., Wei, S.-J., Block, M. L., Wilson, B., Liu, B., & Hong, J.-S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307657200 · Cited by 574 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
“Sepsis leading to organ failure and death: severe inflammatory response syndrome It is well known that one consequence of bacterial infection (sepsis) can be septic shock, that this can be mimicked by the Gram-negative bacterial outer membrane component LPS (lipopolysaccharide), and that in the worst cases this leads…”
BackgroundInfluentialNeuroprotective effects of curcumin
Cole, G. M., Teter, B., & Frautschy, S. A. (2007) · ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY · doi:10.1007/978-0-387-46401-5_8 · Cited by 516 · see citing works
Berberine suppresses proinflammatory responses through AMPK activation in macrophages
Jeong, H. W., Hsu, K. C., Lee, J.-W., Ham, M., Huh, J. Y., Shin, H. J., Kim, W. S., & Kim, J. B. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90599.2008 · Cited by 454 · see citing works
“It has been well established that proinflammatory stimuli such as LPS and TNF- promote an early and acute increase of cellular ROS levels (13, 21) that stimulate MAPK cascade and downstream transcriptional factors to mediate inflammatory responses (13, 21, 50).”
BackgroundResultGouin, O., L’Hérondelle, K., Lebonvallet, N., Gall‐Ianotto, C. L., Sakka, M., Buhé, V., Plée‐Gautier, E., Carré, J., Lefeuvre, L., Misery, L., et al. (2017) · Protein & Cell · doi:10.1007/s13238-017-0395-5 · Cited by 430 · see citing works
Redox regulation of glial inflammatory response to lipopolysaccharide and interferonγ
Pawate, S., Shen, Q., Fan, F., & Bhat, N. R. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20180 · Cited by 428 · see citing works
Eicosapentaenoic Acid Prevents LPS-Induced TNF-α Expression by Preventing NF-κB Activation
Zhao, Y., Joshi-Barve, S., Barve, S., & Chen, L. H. (2004) · Journal of the American College of Nutrition · doi:10.1080/07315724.2004.10719345 · Cited by 405 · see citing works
“Pre-treating cells with antioxidants reduces LPS-induced NF- B transcription activity [51,52] and the activities of upstream Rac1 and protein tyrosine kinases [53,54].”
BackgroundChen, C.-Y., Peng, W.-H., Tsai, K.-D., & Hsu, S.-L. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.09.028 · Cited by 358 · see citing works
“It has been reported that LPS rapidly induces the generation of ROS especially H 2 O 2 in macrophages (Hsu and Wen, 2002; Lu and Wahl, 2005) .”
BackgroundReactive oxygen species mediate RANK signaling in osteoclasts
Ha, H., Bok Kwak, H., Woong Lee, S., Mi Jin, H., Kim, H.-M., Kim, H.-H., & Hee Lee, Z. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.07.035 · Cited by 347 · see citing works
Yuan, H., Perry, C. N., Huang, C., Iwai‐Kanai, E., Carreira, R., Glembotski, C. C., & Gottlieb, R. A. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01051.2008 · Cited by 265 · see citing works
Han, J., Kim, Y. S., Lim, M.-Y., Kim, H. Y., Kong, S., Kang, M., Choo, Y. W., Jun, J. H., Ryu, S., Jeong, H.-Y., et al. (2018) · ACS Nano · doi:10.1021/acsnano.7b09107 · Cited by 261 · see citing works
Kim, D., You, B., Jo, E., Han, S., Simon, M. I., & Lee, S. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009926107 · Cited by 251 · see citing works
“It has been reported that ROS works as an upstream signaling molecule for the expression of proinflammatory cytokines in macrophages (14).”
BackgroundShan, J., Fu, J., Zhao, Z., Kong, X., Huang, H., Luo, L., & Yin, Z. (2009) · International Immunopharmacology · doi:10.1016/j.intimp.2009.04.011 · Cited by 251 · see citing works
Chao, L. K., Hua, K.-F., Hsu, H.-Y., Cheng, S.-S., Lin, I.-F., Chen, C.-J., Chen, S.-T., & Chang, S.-T. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.07.016 · Cited by 250 · see citing works
“MAPKs play important roles in the regulation of cytokines gene expression, such regulation including TNF and IL-1 release within cultured human and murine macrophages (Hsu and Wen, 2002).”
InfluentialSelf-citationIp, W., & Medzhitov, R. M. (2015) · Nature Communications · doi:10.1038/ncomms7931 · Cited by 243 · see citing works
“5b), although this effect is compounded by the effect of NAC on IL-1 gene transcription 31 .”
Importance of MAPK pathways for microglial pro-inflammatory cytokine IL-1β production
Kim, S. H., Smith, C. J., & Eldik, L. J. V. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00126-x · Cited by 234 · see citing works
Mabilleau, G., Bourdon, S., Joly‐Guillou, M., Filmon, R., Baslé, M. F., & Chappard, D. (2005) · Acta Biomaterialia · doi:10.1016/j.actbio.2005.09.004 · Cited by 229 · see citing works
So, H., Kim, H., Lee, J.-H., Park, C., Kim, Y., Kim, E., Kim, J.-K., Yun, K.-J., Lee, K.-M., Lee, H.-Y., et al. (2007) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s10162-007-0084-9 · Cited by 229 · see citing works
“It has also been reported that p38 and ERK pathways play an important role in IL-1b and TNF-a production, respectively (Hsu and Wen 2002; Shi et al. 2002).”
Nagy, L. E. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800803 · Cited by 227 · see citing works
Fujita, K.-I., Maeda, D., Xiao, Q., & Srinivasula, S. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014156108 · Cited by 225 · see citing works
“Given that LPS-induced ROS selectively activates p38, but not JNK (23), we speculated that the ROS-p38 axis might be involved in the induction of p62 and ALIS formation.”
BackgroundInfluentialStudy on the Antiinflammatory Activity of Essential Oil from Leaves of <i>Cinnamomum osmophloeum</i>
Chao, L. K., Hua, K.-F., Hsu, H.-Y., Cheng, S.-S., Liu, J.-Y., & Chang, S.-T. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051151u · Cited by 221 · see citing works
Self-citationSamuvel, D. J., Sundararaj, K. P., Nareika, A., Lopes-Virella, M. F., & Huang, Y. Q. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802059 · Cited by 220 · see citing works
“It has been shown that ROS modulates NF- B-dependent transcription of inflammatory gene expression through their involvement in the early TLR4-mediated cellular responses (45, 46).”
BackgroundMitogen-activated protein kinase pathways in redox signaling
Torrès, M. (2003) · Frontiers in bioscience · doi:10.2741/999 · Cited by 218 · see citing works
Role of reactive oxygen species in LPS‐induced production of prostaglandin E2in microglia
Wang, T., Qin, L., Liu, B., Liu, Y., Wilson, B. C., Eling, T. E., Langenbach, R. I., Taniura, S., & Hong, J. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02242.x · Cited by 218 · see citing works
A Review on Anti-Inflammatory Activity of Phenylpropanoids Found in Essential Oils
Sá, R. D. C. D. S. E., Andrade, L., de Oliveira, R. D. R. B., & de Sousa, D. P. (2014) · Molecules · doi:10.3390/molecules19021459 · Cited by 219 · see citing works
“As these subtypes of MAPKs have been implicated in the regulation of cytokines gene expression, such as TNF and IL-1, as evidenced in culture human and murine macrophages [45], it is believed that cinnamaldehyde inhibitory action on cytokines synthesis could be related to the reduction of ERK 1/2 and JNK 1/2 activatio…”
BackgroundBlockade of NOX2 and STIM1 signaling limits lipopolysaccharide-induced vascular inflammation
Gandhirajan, R. K., Meng, S., Chandramoorthy, H. C. K., Mallilankaraman, K. B., Mancarella, S., Gao, H., Razmpour, R., Yang, X. F., Houser, S. R., Chen, J., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65647 · Cited by 208 · see citing works
“LPS is a major component of the bacterial cell wall widely used to induce ALI in murine models (41).”
InfluentialRyan, K. A., Smith, M. F., Sanders, M. K., & Ernst, P. B. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2123-2130.2004 · Cited by 198 · see citing works
“It has long been known that ROS play a role in intracellular signaling, but the various mechanisms by which the cellular redox state can influence signaling pathways are extremely complex (2, 14, 19).”
BackgroundThakur, V., Pritchard, M. T., McMullen, M. R., Wang, Q., & Nagy, L. E. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.1005613 · Cited by 196 · see citing works
“For example, Hsu and Wen [28] demonstrated that LPS-stimulated ROS production acts via p38 and ERK1/2 MAPKs to enhance interleukin-1 gene expression.”
BackgroundRoles of the NLRP3 inflammasome in the pathogenesis of diabetic nephropathy
Qiu, Y.-Y., & Tang, L. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.11.004 · Cited by 196 · see citing works
“1 murine macrophage cell ine described the significant regulatory role of MAPK signalling olecules, such as p38, JNK and ERK, in the expression of IL-1 and nflammasome components [33,71,72].”
BackgroundGanguly, N., Giang, P. H., Gupta, C., Basu, S. K., Siddiqui, I., Salunke, D. M., & Sharma, P. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100117 · Cited by 183 · see citing works
ATR-dependent radiation-induced γH2AX foci in bystander primary human astrocytes and glioma cells
Burdak‐Rothkamm, S., Short, S. C., Folkard, M., Rothkamm, K., & Prise, K. M. (2006) · Oncogene · doi:10.1038/sj.onc.1209863 · Cited by 190 · see citing works
Plantinga, T., Crișan, T., Oosting, M., van de Veerdonk, F. L., de Jong, D. D., Philpott, D., van der Meer, J. V. D., Girardin, S., Joosten, L., & Netea, M. (2011) · Gut · doi:10.1136/gut.2010.228908 · Cited by 207 · see citing works
Huang, Y. L., Yu, F., Wang, J., & Chen, L. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00458 · Cited by 188 · see citing works
The role of insulin and neurotrophic factor signaling in brain aging and Alzheimer’s Disease
Cole, G. M., & Frautschy, S. A. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.08.009 · Cited by 189 · see citing works
“For example, rac activation is implicated in NADPH oxidase production in reactive microglia (Hsu and Wen, 2002) and COX-2 induction (Wang et al.”
BackgroundBudai, M. M., Varga, A., Milesz, S., Tőzsér, J., & Benkő, S. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.05.005 · Cited by 180 · see citing works
“…Nlrp3 and caspase-1 and studies on J774A.1 murine macrophage cell line described the significant regulatory role of MAPK signaling such as p38, JNK and ERK in the expression of IL-1 and inflammasome components (Bauernfeind et al., 2009; Qiao et al., 2012; Hsu and Wen, 2002; Liao et al., 2012).”
BackgroundWoo, M., Park, J., Choi, I., Kim, W., & Kim, H. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05430.x · Cited by 160 · see citing works
“Cross-regulation between reactive oxygen species production and MMP expression in LPS-stimulated microglia Reactive oxygen species plays an important role in inducing inflammatory mediators in microglia (Hsu and Wen 2002; Jian and Rosenberg 2005).”
BackgroundHsu, H., Hua, K., Lin, C., Lin, C., Hsu, J., & Wong, C. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.10.5989 · Cited by 161 · see citing works
Self-citationKell, D. B., & Pretorius, E. (2015) · Integrative Biology · doi:10.1039/c5ib00158g · Cited by 160 · see citing works
Ballance, W. C., Qin, E. C., Chung, H. J., Gillette, M. U., & Kong, H. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119292 · Cited by 156 · see citing works
“Bacterial lipopolysaccharides (LPS)-mediated ROS, for instance, has been shown to stimulate macrophages to release pro-inflammatory cytokine interleukin 1 (IL-1β) and tumor necrosis factor (TNF) [48].”
BackgroundIncreased production of inflammatory cytokines in mild cognitive impairment
Magaki, S., Mueller, C., DICKSON, C., & Kirsch, W. M. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.09.015 · Cited by 156 · see citing works
“In general, PHA stimulates lymphocyte proliferation, while LPS stimulates monocytes to release IL-1 and TNF-α (Hsu and Wen, 2002; Tyrsted and Munch-Petersen, 1977; Zhu et al., 2000).”
BackgroundTissue factor mediates inflammation
Chu, A. J. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.06.005 · Cited by 156 · see citing works
Tanaka, M., Kishimoto, Y., Sasaki, M., Sato, A., Kamiya, T., Kondo, K., & Iida, K. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9364364 · Cited by 154 · see citing works
“inflammatory mediator expression in macrophages [9].”
Increased susceptibility of MER5 (peroxiredoxin III) knockout mice to LPS-induced oxidative stress
Li, L., Shoji, W., Takano, H., Nishimura, N., Aoki, Y., Takahashi, R., Goto, S., Kaifu, T., Takai, T., & Obinata, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.022 · Cited by 153 · see citing works
Nakanishi, H., & Wu, Z. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.02.001 · Cited by 149 · see citing works
Chen, H., Wu, Y., Zhang, Y., Jin, L., Luo, L., Xue, B., Chen, L., Zhang, X., & Yin, Z. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.066 · Cited by 149 · see citing works
Role of selenium-containing proteins in T-cell and macrophage function
Carlson, B. A., Yoo, M., Shrimali, R. K., Irons, R., Gladyshev, V. N., Hatfield, D. L., & Park, J. M. (2010) · Proceedings of The Nutrition Society · doi:10.1017/s002966511000176x · Cited by 143 · see citing works
“The fact that several inflammatory stimuli such as lipopolysaccharide (LPS) cause transient ROS accumulation as part of cellular signalling events((32,33)), and several selenoproteins, e.”
BackgroundAwareness and current knowledge of Parkinson’s disease: a neurodegenerative disorder
Khan, A. U., Akram, M., Daniyal, M., & Zainab, R. (2018) · International Journal of Neuroscience · doi:10.1080/00207454.2018.1486837 · Cited by 145 · see citing works
“The existence of synuclein accumulation in the SN was identified, whereas neither group revealed an advanced motor malfunction [175].”
BackgroundGasdermin D pore-forming activity is redox-sensitive
Devant, P., Boršić, E., Ngwa, E. M., Xiao, H., Chouchani, E. T., Thiagarajah, J. R., Hafner‐Bratkovič, I., Evavold, C. L., & Kagan, J. C. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112008 · Cited by 145 · see citing works
Obstacles against the Marketing of Curcumin as a Drug
Hassanzadeh, K., Buccarello, L., Dragotto, J., Mohammadi, A., Corbo, M., & Feligioni, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186619 · Cited by 145 · see citing works
ICAM-1 induction by TNFα and IL-6 is mediated by distinct pathways via Rac in endothelial cells
Wung, B., Ni, C., & Wang, D. L. (2005) · Journal of Biomedical Science · doi:10.1007/s11373-004-8170-z · Cited by 138 · see citing works
“Inhibition of Rac1mediated ROS production has been shown to attenuate cytokine-induced endothelial responses [ 47 , 48].”
BackgroundThakur, V., Pritchard, M. T., McMullen, M. R., & Nagy, L. E. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00553.2005 · Cited by 138 · see citing works
“LPS-stimulated production of ROS has been implicated in the activation of ERK1/2 in macrophages and monocytes (12, 17).”
BackgroundJanus kinase 2 is involved in lipopolysaccharide-induced activation of macrophages
Okugawa, S., Ota, Y., Kitazawa, T., Nakayama, K., Yanagimoto, S., Tsukada, K., Kawada, M., & Kimura, S. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00026.2003 · Cited by 132 · see citing works
“A recent study demonstrated that the PI3K/Akt pathway positively regulates NF- B-dependent gene expression (21, 51).”
BackgroundInfluentialCyclooxygenase‐2 Regulates NLRP3 Inflammasome‐Derived IL‐1β Production
Hua, K., Chou, J., Ka, S., Tasi, Y., Chen, A., Wu, S., Chiu, H., Wong, W.-T., Wang, Y., Tsai, C., et al. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24815 · Cited by 132 · see citing works
Roy, A., Jana, A., Yatish, K., Freidt, M. B., Fung, Y. K., Martinson, J., & Pahan, K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.026 · Cited by 131 · see citing works
Nair, V., Bang, W. Y., Schreckinger, E., Andarwulan, N., & Cisneros‐Zevallos, L. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b00928 · Cited by 130 · see citing works
So, H., Kim, H., Kim, Y., Kim, E., Pae, H., Chung, H., Kim, H. J., Kwon, K., Lee, K., Lee, H.-Y., et al. (2008) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s10162-008-0126-y · Cited by 130 · see citing works
“For example, it has been reported that the p38 and ERK pathways play an important role in IL-1β and TNF-α production, respectively (Hsu and Wen 2002; Shi et al. 2002).”
Pharmacologic Overview of Chlorogenic Acid and its Metabolites in Chronic Pain and Inflammation
Bağdaş, D., Gül, Z., Meade, J. A., Çam, B., Çinkılıç, N., & Gurun, M. S. (2019) · Current Neuropharmacology · doi:10.2174/1570159x17666191021111809 · Cited by 126 · see citing works
Park, C. M., Jin, K.-S., Lee, Y., & Song, Y. S. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.04.007 · Cited by 122 · see citing works
“This was stimulated by LPS treatment in RAW 264.7 cells as previously described (Hsu and Wen, 2002) and free radical production was analyzed using DCF-DA.”
MethodInfluentialNamba, T., Tanaka, K., Ito, Y., Ishihara, T., Hoshino, T., Gotoh, T., Endo, M., Sato, K., & Mizushima, T. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080864 · Cited by 121 · see citing works
“Treatment of WT macrophages with LPS stimulated ROS production (Figure 8C), as has been described previously.(46) However, this stimulation was not clearly observed in CHOPnull macrophages, indicating that CHOP is responsible for LPS-stimulated ROS production (Figure 8C).”
MethodOuyang, Y., Zhao, J., & Wang, S. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.12.032 · Cited by 119 · see citing works
Endosomal Nox2 Facilitates Redox-Dependent Induction of NF-κB by TNF-α
Li, Q., Spencer, N. Y., Oakley, F. D., Buettner, G. R., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2407 · Cited by 120 · see citing works
“…be induced in cells after receptor stimulation with various ligands such as tumor necrosis factor alpha (TNF-a ) (12, 39), lipopolysaccharide (LPS) (24, 51), angiotensin II (18), platelet-derived growth factor (PDGF) (56), insulin (37), epidermal growth factor (EGF) (2), and interleukin-1 b (IL-1…”
Kim, J. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2003.11.004 · Cited by 120 · see citing works
Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops
Kondo, N., Ishii, Y., Kwon, Y.-W., Tanito, M., Horita, H., Nishinaka, Y., Nakamura, H., & Yodoi, J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.442 · Cited by 116 · see citing works
“In support of this hypothesis, it is reported that LPS-induced pro-IL-1 production and IL-1 secretion corresponded to the production of ROS and activation of c-Jun N-terminal kinase, p38, and extracellular signal-regulated kinase (33).”
BackgroundMcMullen, M. R., Pritchard, M. T., Wang, Q., Millward, C. A., Croniger, C. M., & Nagy, L. E. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.02.065 · Cited by 116 · see citing works
Ji, Y. S., Yin, W., Liang, Y., Sun, L., Yin, Y., & Zhang, W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051579 · Cited by 115 · see citing works
“, reactive oxidative species (ROS) and nitric oxide (NO)) [4,5].”
BackgroundHuang, B., Lin, C.-H., Chen, H., Lin, J., Cheng, Y., & Kao, S. (2014) · DNA and Cell Biology · doi:10.1089/dna.2014.2630 · Cited by 113 · see citing works
“LPS binds to toll-like receptor (TLR)-4 and induces secretion of a variety of proin-flammatory cytokines, such as interleukin (IL)-1 b , IL-6, and tumor necrosis factor (TNF)- a (Raabe et al. , 1998; Hsu and Wen, 2002).”
Hsu, H.-Y., Lin, T., Lu, M., Leng, P.-J., Tsao, S.-M., & Wu, Y. (2017) · Scientific Reports · doi:10.1038/srep44990 · Cited by 113 · see citing works
Self-citationZeng, K., Fu, H. Y., Liu, G.-X., & Wang, X. (2010) · International Immunopharmacology · doi:10.1016/j.intimp.2010.03.010 · Cited by 111 · see citing works
Xie, S., Zhou, W., Tian, L., Niu, J., & Liu, Y. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.05.033 · Cited by 110 · see citing works
Extracellular Superoxide Dismutase Attenuates Lipopolysaccharide-Induced Neutrophilic Inflammation
Bowler, R. P., Nicks, M., Tran, K. C., Tanner, G., Chang, L., Young, S. K., & Worthen, G. S. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0057oc · Cited by 110 · see citing works
“The signaling pathways by which this occurs are not completely known, but may include extracellular signal-related kinase and p38 (45) or NF- B, activator protein–1, and cyclic adenosine monophosphate response element binding protein (47).”
BackgroundJhun, B. S., Jin, Q., Oh, Y. T., Kim, S. S., Kong, Y., Cho, Y. H., Ha, J., Baik, H. H., & Kang, I. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.04.035 · Cited by 108 · see citing works
Orthogonal Activation of RNA‐Cleaving DNAzymes in Live Cells by Reactive Oxygen Species
Xiao, L., Gu, C., & Xiang, Y. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201908105 · Cited by 107 · see citing works
Liao, P., Chien, S., Ho, C., Wang, E. I., Lee, S.-C., Kuo, Y., Jeyashoke, N., Chen, J., Dong, W.-C., Chao, L. K., et al. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf102812t · Cited by 105 · see citing works
Komatsu, W., Kishi, H., Yagasaki, K., & Ohhira, S. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.06.023 · Cited by 105 · see citing works
“It has been reported that LPS rapidly induces the generation of reactive oxygen species in macrophages (Hsu and Wen, 2002).”
BackgroundUltrasmall Antioxidant Cerium Oxide Nanoparticles for Regulation of Acute Inflammation
Kim, J., Hong, G., Mazaleuskaya, L., Hsu, J. C., Rosario‐Berríos, D. N., Großer, T., Cho-Park, P. F., & Cormode, D. P. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c16126 · Cited by 104 · see citing works
Kim, A.-R., Lee, M., Shin, T.-S., Hua, H., Jang, B., Choi, J., Byun, D., Utsuki, T., Ingram, D. K., & Kim, H. (2011) · Toxicology in Vitro · doi:10.1016/j.tiv.2011.09.012 · Cited by 103 · see citing works
“These classical MAPKs, extracellular signal regulated kinase (ERKs), p38 MAPK, and c-Jun NH2-terminal kinase (JNKs) have been implicated in the transcriptional regulation of inflammatory genes (Herlaar and Brown, 1999).”
InfluentialXie, Q., SHEN, W.-W., Zhong, J., Huang, C., Zhang, L., & Li, J. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1755 · Cited by 103 · see citing works
“The NLRP3 inflammasome is activated in response to a variety of signals that include pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) (6).”
InfluentialDu, J., Xu, R., Hu, Z., Tian, Y., Zhu, Y., Gu, L., & Zhou, L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025213 · Cited by 103 · see citing works
“This result is consistent with findings showing that NAC inhibited Rac1 activity in response to LPS in macrophages [56].”
ResultMatsuda, T., Omori, K., Vuong, T., Pascual, M., Valiente, L., Ferreri, K., Todorov, I., Kuroda, Y., Smith, C. V., KANDEEL, F. R., et al. (2005) · American Journal of Transplantation · doi:10.1046/j.1600-6143.2004.00716.x · Cited by 103 · see citing works
“Their ability to suppress pro-inflammatory mediators, such as IL-1b, TNF-a and IL-6, has also been well documented in the cells of the monocyte–macrophage lineage (15,16,36).”
Chao, L. K., Liao, P., Ho, C., Wang, E. I., Chuang, C.-C., Chiu, H.-W., Hung, L., & Hua, K. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf904207m · Cited by 102 · see citing works
Gangliosides activate microglia via protein kinase C and NADPH oxidase
Min, K., Pyo, H., Yang, M., Ji, K., Jou, I., & Joe, E.-H. (2004) · Glia · doi:10.1002/glia.20069 · Cited by 101 · see citing works
“ROS play an important role in inducing inflammatory mediators in microglia (Kang et al., 2001b; Hsu and Wen, 2002).”
BackgroundKelk, P., Abd, H., Claesson, R., Sandström, G., Sjöstedt, A. B., & Johansson, A. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.6 · Cited by 100 · see citing works
Chen, Y.-F., Wang, Y., Huang, W.-S., Lee, M.-M., Wood, W. G., Leung, Y., & Tsai, H.-Y. (2016) · NeuroMolecular Medicine · doi:10.1007/s12017-016-8395-9 · Cited by 99 · see citing works
“LPS induces PGE2 production in humanmicroglia through COX2 induction (Hsu and Wen 2002).”
BackgroundLiao, P., Chao, L. K., Chou, J., Dong, W.-C., Lin, C.-N., Lin, C.-Y., Chen, A., Ka, S., Ho, C., & Hua, K. (2012) · Inflammation Research · doi:10.1007/s00011-012-0555-2 · Cited by 97 · see citing works
“Interleukin (IL)-1b is one of the important cytokines rapidly synthesized in an inactive immature form (precursor of IL-1b, proIL-1b) via transcriptional activation in lipopolysaccharide (LPS)-activated macrophages [1].”
Erickson, M. A., Hansen, K. M., & Banks, W. A. (2012) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2012.07.003 · Cited by 100 · see citing works
“ROS produced in response to inflammatory stimuli can exacerbate inflammation by activating a number of signaling molecules, including NFk-B, AP-1 MAPK (Hsu and Wen, 2002; Lo et al., 1996; Morgan and Liu, 2011), and promoting inflammasome activation (Martinon, 2010).”
Robinson, N. A., Gopikrishna, G., Baranski, M., Katneni, V. K., Shekhar, M. S., Shanmugakarthik, J., Jothivel, S., Gopal, C., Ravichandran, P., Gitterle, T., et al. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-731 · Cited by 98 · see citing works
“Mitogen activated protein kinases Protein kinase signal transduction pathways, including mitogen-activated protein kinases, have been shown to have important roles in the regulation of cytokine gene expression [58-60], particularly interleukin-1, which is a potent inflammatory cytokine regulating host defence and immu…”
BackgroundLiposphere mediated topical delivery of thymoquinone in the treatment of psoriasis
Jain, A., Pooladanda, V., Bulbake, U., Doppalapudi, S., Rafeeqi, T. A., Godugu, C., & Khan, W. (2017) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2017.06.009 · Cited by 97 · see citing works
The Role of Lipopolysaccharide on the Electrochemical Behavior of Titanium
Barão, V. A. R., Mathew, M. T., Assunção, W. G., Yuan, J. C., Wimmer, M. A., & Sukotjo, C. (2011) · Journal of Dental Research · doi:10.1177/0022034510396880 · Cited by 97 · see citing works
“…as key defenders of the organism and have been involved in the mediation of inflammatory responses by producing pro-inflammatory cytokines and reactive oxygen species in the presence of either bacterial components such as LPS or biomaterial particles (Hsu and Wen, 2002; Mabilleau et al., 2006).”
BackgroundLi, Y., Wei, S., Chu, H., Jian, H., Anand, A., Nain, A., Huang, Y., Chang, H., Huang, C., & Lai, J. (2022) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.135315 · Cited by 96 · see citing works
Regulation of macrophage activation in alcoholic liver disease
Thakur, V., McMullen, M. R., Pritchard, M. T., & Nagy, L. E. (2007) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2006.04650.x · Cited by 93 · see citing works
Zhou, Y., Wang, J., Yang, W., Qi, X., Lan, L., Luo, L., & Yin, Z. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.04.026 · Cited by 91 · see citing works
Microglial cells and Parkinson’s disease
Li, Q., & Flood, P. M. (2008) · Immunologic Research · doi:10.1007/s12026-008-8018-0 · Cited by 91 · see citing works
“Furthermore, studies with LPS-activated macrophages have demonstrated that the generation of ROS is an upstream event which regulates the production of other pro-inXammatory factors such as TNF and IL-1 through its regulation of the transcription factor NF-kB [46, 47 ].”
BackgroundLin, F., Chen, Y., Tasi, J.-S., Chen, J., Yang, T.-L., Wang, H.-J., Li, C., Chen, Y., & Lin, S. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000247259.01257.b3 · Cited by 91 · see citing works
Mahlknecht, U., Will, J., Varin, A., Hoelzer, D. F., & Herbein, G. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3979 · Cited by 89 · see citing works
“We also observed that HDAC3 represses the IL-1 gene expression and the IL-1 protein production in LPS-treated THP-1 cells (data not shown), indicating that HDAC3 represses the secretion of proinflammatory cytokines, such as TNF and IL-1 , in activated monocytic cells (46).”
BackgroundRoca, M. G., Weichert, M., Siegmund, U., Tudzynski, P., & Fleißner, A. (2011) · Fungal Biology · doi:10.1016/j.funbio.2011.12.007 · Cited by 89 · see citing works
- 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)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review