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Activation of the JAK-STAT pathway by reactive oxygen species
Abstract
Reactive oxygen species (ROS) play an important role in the pathogenesis of many human diseases, including the acute respiratory distress syndrome, Parkinson’s disease, pulmonary fibrosis, and Alzheimer’s disease. In mammalian cells, several genes known to be induced during the immediate early response to growth factors, including the protooncogenes c- fos and c- myc, have also been shown to be induced by ROS. We show that members of the STAT family of transcription factors, including STAT1 and STAT3, are activated in fibroblasts and A-431 carcinoma cells in response to H 2 O 2. This activation occurs within 5 min, can be inhibited by antioxidants, and does not require protein synthesis. STAT activation in these cell lines is oxidant specific and does not occur in response to superoxide- or nitric oxide-generating stimuli. Buthionine sulfoximine, which depletes intracellular glutathione, also activates the STAT pathway. Moreover, H 2 O 2 stimulates the activity of the known STAT kinases JAK2 and TYK2. Activation of STATs by platelet-derived growth factor (PDGF) is significantly inhibited by N-acetyl-l-cysteine and diphenylene iodonium, indicating that ROS production contributes to STAT activation in response to PDGF. These findings indicate that the JAK-STAT pathway responds to intracellular ROS and that PDGF uses ROS as a second messenger to regulate STAT activation.
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Cites
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor
Schindler, C., Shuai, K., Prezioso, V. R., & Darnell, J. E. (1992) · Science · doi:10.1126/science.1496401 · Cited by 899
Caldenhoven, E., van Dijk, T. B., Solari, R., Armstrong, J., Raaijmakers, J. A. M., Lammers, J.-W. J., Koenderman, L., & de Groot, R. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13221 · Cited by 373
Wu, Y. Y., & Bradshaw, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13023 · Cited by 100
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Oxidative stress, inflammation, and cancer: How are they linked?
Reuter, S., Gupta, S. C., Chaturvedi, M. M., & Aggarwal, B. B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.006 · Cited by 5,441
Cuzzocrea, S., Riley, D. P., Caputi, A. P., & Salvemini, D. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01484-4 · Cited by 1,087
Regulation of PDGF and its receptors in fibrotic diseases
Bonner, J. C. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.03.006 · Cited by 768
Bharath, L. P., Agrawal, M., McCambridge, G., Nicholas, D. A., Hasturk, H., Liu, J., Jiang, K., Liu, R., Guo, Z., Deeney, J., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.015 · Cited by 614
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495
Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1
Arnold, R. S., Shi, J., Murad, E., Whalen, A. M., Sun, C. Q., Polavarapu, R., Parthasarathy, S., Petros, J. A., & Lambeth, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101505898 · Cited by 486
Oxidative stress in the pathology and treatment of systemic lupus erythematosus
Perl, A. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.147 · Cited by 358
Subramanian Vignesh, K., Landero Figueroa, J. A., Porollo, A., Caruso, J. A., & Deepe, G. S. (2013) · Immunity · doi:10.1016/j.immuni.2013.09.006 · Cited by 230
Hydrogen peroxide increases extracellular matrix mRNA through TGF-β in human mesangial cells
Iglesias-de la Cruz, M. C., Ruiz-Torres, P., Alcamí, J., Díez-Marqués, L., Ortega-Velázquez, R., Chen, S., Rodríguez-Puyol, M., Ziyadeh, F. N., & Rodríguez-Puyol, D. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00469.x · Cited by 217
Nox5 mediates PDGF-induced proliferation in human aortic smooth muscle cells
Jay, D. B., Papaharalambus, C. A., Seidel-Rogol, B., Dikalova, A. E., Lassègue, B., & Griendling, K. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.024 · Cited by 166
Cai, H., Davis, M. E., Drummond, G. R., & Harrison, D. G. (2001) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/hq1001.097028 · Cited by 160
Ncf1 polymorphism reveals oxidative regulation of autoimmune chronic inflammation
Holmdahl, R., Sareila, O., Olsson, L. M., Bäckdahl, L., & Wing, K. (2016) · Immunological Reviews · doi:10.1111/imr.12378 · Cited by 131
JANUS under stress—Role of JAK/STAT signaling pathway in vascular diseases
Grote, K., Luchtefeld, M., & Schieffer, B. (2005) · Vascular Pharmacology · doi:10.1016/j.vph.2005.08.021 · Cited by 128
Portugal, M., Barak, V., Ginsburg, I., & Kohen, R. (2007) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2007.05.010 · Cited by 121
Cardoso, A. A., Jiang, Y., Luo, M., Reed, A. M., Shahda, S., He, Y., Maitra, A., Kelley, M. R., & Fishel, M. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047462 · Cited by 97
Autoschizis: a novel cell death
Jamison, J. M., Gilloteaux, J., Taper, H. S., Calderon, P. B., & Summers, J. L. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)00904-8 · Cited by 87
A STAT3 dimer formed by inter-chain disulphide bridging during oxidative stress
Li, L., & Shaw, P. E. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.014 · Cited by 79
Chimenti, M. S., Sunzini, F., Fiorucci, L., Botti, E., Fonti, G. L., Conigliaro, P., Triggianese, P., Costa, L., Caso, F., Giunta, A., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02363 · Cited by 77
Nucleus, mitochondrion, or reticulum? STAT3 à La Carte
Avalle, L., & Poli, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092820 · Cited by 74
Role of mtDNA disturbances in the pathogenesis of Alzheimer’s and Parkinson’s disease
Antonyová, V., Kejík, Z., Brogyányi, T., Kaplánek, R., Pajková, M., Talianová, V., Hromádka, R., Masařík, M., Sýkora, D., Mikšátková, L., et al. (2020) · DNA Repair · doi:10.1016/j.dnarep.2020.102871 · Cited by 45
Song, N.-Y., Lee, Y.-H., Na, H.-K., Baek, J.-H., & Surh, Y.-J. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.02.001 · Cited by 36
Beyond M1/M2: The role of reactive oxygen species in liver fibrosis and immune modulation
Lu, H., Huang, J., Wang, Y.-C., Casals, E., Casals, G., & Zeng, M. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103933 · Cited by 19
Interleukin-6 regulation of direct lung ischemia reperfusion injury
Farivar, A. S., Merry, H. E., Fica-Delgado, M. J., McCourtie, A. S., Mackinnon-Patterson, B. C., & Mulligan, M. S. (2006) · The Annals of Thoracic Surgery · doi:10.1016/j.athoracsur.2006.03.060 · Cited by 15
Metadata
- Authors
- Simon, A. R., Rai, U., Fanburg, B. L., & Cochran, B. H.
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 1998-12-01
- Volume
- 275
- Issue
- 6
- Pages
- C1640-C1652
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W1827885532
- Cited by
- 598
- References
- 7
- FWCI
- 5.77
- Type
- journal article
- Language
- en
- Open access
- closed
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