The DOI matches its Crossref record; 182 of the 182 references it cites were found in a registry or an index.
Regulation of superoxide dismutase genes: Implications in disease
Open accessAbstract
Numerous short-lived and highly reactive oxygen species (ROS) such as O2·- (superoxide), ·OH (hydroxyl radical), and H2O2 (hydrogen peroxide) are continuously generated in vivo. Depending upon concentration, location and intracellular conditions, ROS can cause toxicity or act as signaling molecules. The cellular levels of ROS are controlled by antioxidant enzymes and small molecule antioxidants. As major antioxidant enzymes, superoxide dismutases (SODs), including copper-zinc superoxide dismutase (Cu/ZnSOD), manganese superoxide dismutase (MnSOD) and extracellular superoxide dismutase (ECSOD), play a crucial role in scavenging O2·-. This review focuses on the regulation of the genes (sods) coding for these enzymes with an emphasis on human genes. Current knowledge about sods structure and their regulation is summarized and depicted as diagrams. Studies to date on genes coding for Cu/ZnSOD (sod1) are mostly focused on alteration in the coding region and their associations with Amyotrophic Lateral Sclerosis (ALS). Evaluation of nucleotide sequences reveals that regulatory elements of the sod2 gene reside in both the non-coding and coding regions. Changes associated with sod2 lead to alteration in expression levels as well as protein function. We also discuss the structural basis for the changes in SOD expression associated with pathological conditions and where more work is needed to establish the relationship between SODs and diseases.
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“Oxidative stress caused by the imbalance between reactive oxygen species (ROS) or reactive nitrogen species (RNS) and biological antioxidant system can lead to modification of macromolecules such as DNA, lipid and protein [1-3].”
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Mechanism of Oxidative Stress in Neurodegeneration
Gandhi, S., & Abramov, A. Y. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/428010 · Cited by 960
Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860
Ulvan: A systematic review of extraction, composition and function
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Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572
Anticancer Activity of Metal Complexes: Involvement of Redox Processes
Jungwirth, U., Kowol, C. R., Keppler, B. K., Hartinger, C. G., Berger, W., & Heffeter, P. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3663 · Cited by 554
Metadata
- Authors
- Miao, L., & St. Clair, D. K.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2009-08
- Volume
- 47
- Issue
- 4
- Pages
- 344-356
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2037434205
- Cited by
- 912
- References
- 182
- FWCI
- 15.60
- Type
- journal article
- Language
- en
- Open access
- green
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