Biology:SOD3
 Generic protein structure example |
Extracellular superoxide dismutase [Cu-Zn] is an enzyme that in humans is encoded by the SOD3 gene.
This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.[1]
Among black garden ants (Lasius niger), the lifespan of queens is an order of magnitude greater than of workers despite no systematic nucleotide sequence difference between them.[2] The SOD3 gene was found to be the most differentially over-expressed gene in the brains of queen vs worker ants. This finding raises the possibility that SOD3 antioxidant activity plays a key role in the striking longevity of social insect queens.[2]
References
- ↑ "Entrez Gene: SOD3 superoxide dismutase 3, extracellular". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6649.
- ↑ 2.0 2.1 Lucas ER, Keller L. Elevated expression of ageing and immunity genes in queens of the black garden ant. Exp Gerontol. 2018 Jul 15;108:92-98. doi: 10.1016/j.exger.2018.03.020. Epub 2018 Apr 3. PMID: 29625209
Further reading
- "Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression". Free Radical Biology & Medicine 33 (3): 337–49. August 2002. doi:10.1016/S0891-5849(02)00905-X. PMID 12126755.
- "Vascular protection: superoxide dismutase isoforms in the vessel wall". Arteriosclerosis, Thrombosis, and Vascular Biology 24 (8): 1367–73. August 2004. doi:10.1161/01.ATV.0000133604.20182.cf. PMID 15166009.
- "Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody". Clinica Chimica Acta; International Journal of Clinical Chemistry 212 (3): 89–102. November 1992. doi:10.1016/0009-8981(92)90176-Q. PMID 1477980.
- "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro". Free Radical Biology & Medicine 13 (3): 205–10. September 1992. doi:10.1016/0891-5849(92)90016-A. PMID 1505778.
- "Expression of extracellular superoxide dismutase by human cell lines". The Biochemical Journal 266 (1): 213–9. February 1990. doi:10.1042/bj2660213. PMID 2106874.
- "Regional localization of human extracellular superoxide dismutase gene to 4pter-q21". Genomics 8 (4): 736–8. December 1990. doi:10.1016/0888-7543(90)90264-U. PMID 2276747.
- "Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase". Proceedings of the National Academy of Sciences of the United States of America 84 (18): 6340–4. September 1987. doi:10.1073/pnas.84.18.6340. PMID 3476950. Bibcode: 1987PNAS...84.6340H.
- "Extracellular superoxide dismutase in human tissues and human cell lines". The Journal of Clinical Investigation 74 (4): 1398–403. October 1984. doi:10.1172/JCI111550. PMID 6541229.
- "Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum". The Japanese Journal of Human Genetics 40 (2): 177–84. June 1995. doi:10.1007/BF01883574. PMID 7662997.
- "Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene". Genomics 22 (1): 162–71. July 1994. doi:10.1006/geno.1994.1357. PMID 7959763.
- "10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain". The Journal of Biological Chemistry 269 (29): 19163–6. July 1994. doi:10.1016/S0021-9258(17)32289-5. PMID 8034674.
- "Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface". The Biochemical Journal 313 ( Pt 1) (1): 235–9. January 1996. doi:10.1042/bj3130235. PMID 8546689.
- "Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase". The Biochemical Journal 317 ( Pt 1) (1): 51–7. July 1996. doi:10.1042/bj3170051. PMID 8694786.
- "An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases". Journal of Biochemistry 120 (1): 184–8. July 1996. doi:10.1093/oxfordjournals.jbchem.a021383. PMID 8864862.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. September 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis". The Journal of Biological Chemistry 274 (21): 14818–22. May 1999. doi:10.1074/jbc.274.21.14818. PMID 10329680.
- "Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase". The Journal of Biological Chemistry 277 (19): 16505–11. May 2002. doi:10.1074/jbc.M105409200. PMID 11861638.
- "The expression of extracellular-superoxide dismutase is increased by lysophosphatidylcholine in human monocytic U937 cells". Atherosclerosis 163 (2): 223–8. August 2002. doi:10.1016/S0021-9150(02)00007-2. PMID 12052468.
- "Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening". The Journal of Biological Chemistry 278 (9): 6824–30. February 2003. doi:10.1074/jbc.M207939200. PMID 12475988.
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