| 释义 |
- References
- Further reading
{{Infobox_gene}}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] References 1. ^{{cite web | title = Entrez Gene: SOD3 superoxide dismutase 3, extracellular| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6649| accessdate = }}
Further reading {{refbegin | 2}}- {{cite journal | vauthors = Zelko IN, Mariani TJ, Folz RJ | title = Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression | journal = Free Radical Biology & Medicine | volume = 33 | issue = 3 | pages = 337–49 | date = August 2002 | pmid = 12126755 | doi = 10.1016/S0891-5849(02)00905-X }}
- {{cite journal | vauthors = Faraci FM, Didion SP | title = Vascular protection: superoxide dismutase isoforms in the vessel wall | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 24 | issue = 8 | pages = 1367–73 | date = August 2004 | pmid = 15166009 | doi = 10.1161/01.ATV.0000133604.20182.cf }}
- {{cite journal | vauthors = Adachi T, Ohta H, Yamada H, Futenma A, Kato K, Hirano K | title = Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 212 | issue = 3 | pages = 89–102 | date = November 1992 | pmid = 1477980 | doi = 10.1016/0009-8981(92)90176-Q }}
- {{cite journal | vauthors = Adachi T, Ohta H, Hayashi K, Hirano K, Marklund SL | title = The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro | journal = Free Radical Biology & Medicine | volume = 13 | issue = 3 | pages = 205–10 | date = September 1992 | pmid = 1505778 | doi = 10.1016/0891-5849(92)90016-A }}
- {{cite journal | vauthors = Marklund SL | title = Expression of extracellular superoxide dismutase by human cell lines | journal = The Biochemical Journal | volume = 266 | issue = 1 | pages = 213–9 | date = February 1990 | pmid = 2106874 | pmc = 1131117 | doi = }}
- {{cite journal | vauthors = Hendrickson DJ, Fisher JH, Jones C, Ho YS | title = Regional localization of human extracellular superoxide dismutase gene to 4pter-q21 | journal = Genomics | volume = 8 | issue = 4 | pages = 736–8 | date = December 1990 | pmid = 2276747 | doi = 10.1016/0888-7543(90)90264-U }}
- {{cite journal | vauthors = Hjalmarsson K, Marklund SL, Engström A, Edlund T | title = Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 18 | pages = 6340–4 | date = September 1987 | pmid = 3476950 | pmc = 299071 | doi = 10.1073/pnas.84.18.6340 }}
- {{cite journal | vauthors = Marklund SL | title = Extracellular superoxide dismutase in human tissues and human cell lines | journal = The Journal of Clinical Investigation | volume = 74 | issue = 4 | pages = 1398–403 | date = October 1984 | pmid = 6541229 | pmc = 425307 | doi = 10.1172/JCI111550 }}
- {{cite journal | vauthors = Yamada H, Yamada Y, Adachi T, Goto H, Ogasawara N, Futenma A, Kitano M, Hirano K, Kato K | title = Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum | journal = The Japanese Journal of Human Genetics | volume = 40 | issue = 2 | pages = 177–84 | date = June 1995 | pmid = 7662997 | doi = 10.1007/BF01883574 }}
- {{cite journal | vauthors = Folz RJ, Crapo JD | title = Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene | journal = Genomics | volume = 22 | issue = 1 | pages = 162–71 | date = July 1994 | pmid = 7959763 | doi = 10.1006/geno.1994.1357 }}
- {{cite journal | vauthors = Sandström J, Nilsson P, Karlsson K, Marklund SL | title = 10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain | journal = The Journal of Biological Chemistry | volume = 269 | issue = 29 | pages = 19163–6 | date = July 1994 | pmid = 8034674 | doi = }}
- {{cite journal | vauthors = Adachi T, Yamada H, Yamada Y, Morihara N, Yamazaki N, Murakami T, Futenma A, Kato K, Hirano K | title = Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface | journal = The Biochemical Journal | volume = 313 ( Pt 1) | issue = 1 | pages = 235–9 | date = January 1996 | pmid = 8546689 | pmc = 1216888 | doi = }}
- {{cite journal | vauthors = Oury TD, Crapo JD, Valnickova Z, Enghild JJ | title = Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase | journal = The Biochemical Journal | volume = 317 ( Pt 1) | issue = 1 | pages = 51–7 | date = July 1996 | pmid = 8694786 | pmc = 1217485 | doi = }}
- {{cite journal | vauthors = Adachi T, Morihara N, Yamazaki N, Yamada H, Futenma A, Kato K, Hirano K | title = An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases | journal = Journal of Biochemistry | volume = 120 | issue = 1 | pages = 184–8 | date = July 1996 | pmid = 8864862 | doi = 10.1093/oxfordjournals.jbchem.a021383 }}
- {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = September 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
- {{cite journal | vauthors = Enghild JJ, Thogersen IB, Oury TD, Valnickova Z, Hojrup P, Crapo JD | title = The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis | journal = The Journal of Biological Chemistry | volume = 274 | issue = 21 | pages = 14818–22 | date = May 1999 | pmid = 10329680 | doi = 10.1074/jbc.274.21.14818 }}
- {{cite journal | vauthors = Bowler RP, Nicks M, Olsen DA, Thøgersen IB, Valnickova Z, Højrup P, Franzusoff A, Enghild JJ, Crapo JD | title = Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 19 | pages = 16505–11 | date = May 2002 | pmid = 11861638 | doi = 10.1074/jbc.M105409200 }}
- {{cite journal | vauthors = Yamamoto M, Hara H, Adachi T | title = The expression of extracellular-superoxide dismutase is increased by lysophosphatidylcholine in human monocytic U937 cells | journal = Atherosclerosis | volume = 163 | issue = 2 | pages = 223–8 | date = August 2002 | pmid = 12052468 | doi = 10.1016/S0021-9150(02)00007-2 }}
- {{cite journal | vauthors = Serra V, von Zglinicki T, Lorenz M, Saretzki G | title = Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening | journal = The Journal of Biological Chemistry | volume = 278 | issue = 9 | pages = 6824–30 | date = February 2003 | pmid = 12475988 | doi = 10.1074/jbc.M207939200 }}
{{refend}}{{Other oxidoreductases}}{{gene-4-stub}} 3 : Oxidoreductases|Copper enzymes|Zinc enzymes |