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Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α
Open accessAbstract
Mammalian tissues express three immunologically distinct peroxiredoxin (Prx) proteins (Prx I, II, and III), which are the products of distinct genes. With the use of recombinant proteins Prx I, II, and III, all have now been shown to possess peroxidase activity and to rely on Trx as a source of reducing equivalents for the reduction of H2O2. Prx I and II are cytosolic proteins, whereas Prx III is localized in mitochondria. Transient overexpression of Prx I or II in cultured cells showed that they were able to eliminate the intracellular H2O2 generated in response to growth factors. Moreover, the activation of nuclear factor kappaB (NFkappaB) induced by extracellularly added H2O2 or tumor necrosis factor-alpha was blocked by overproduction of Prx II. These results suggest that, together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition, Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2.
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Cites
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
Cited by
Oxidative Stress: An Essential Factor in the Pathogenesis of Gastrointestinal Mucosal Diseases
Bhattacharyya, A., Chattopadhyay, R., Mitra, S., & Crowe, S. E. (2014) · Physiological Reviews · doi:10.1152/physrev.00040.2012 · Cited by 2,484
Histone deacetylase inhibitors: molecular mechanisms of action
Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542
Halliwell, B. (2001) · Drugs & Aging · doi:10.2165/00002512-200118090-00004 · Cited by 1,502
Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409
Self-citationHydrogen peroxide in the human body
Halliwell, B., Clement, M. V., & Long, L. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02197-9 · Cited by 1,075
Metadata
- Authors
- Kang, S. W., Chae, H. Z., Seo, M. S., Kim, K., Baines, I. C., & Rhee, S. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-03
- Volume
- 273
- Issue
- 11
- Pages
- 6297-6302
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2017265125
- Cited by
- 692
- References
- 1
- FWCI
- 13.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kang, S. W., Chae, H. Z., Seo, M. S., Kim, K., Baines, I. C., & Rhee, S. G. (1998). Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.11.6297
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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