SOD3

SOD3

Superoxide dismutase 3, extracellular, also known as SOD3, is a human gene.

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summary_text = 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.cite web | title = Entrez Gene: SOD3 superoxide dismutase 3, extracellular| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6649| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=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 Radic. Biol. Med. |volume=33 |issue= 3 |pages= 337–49 |year= 2003 |pmid= 12126755 |doi=
*cite journal | author=Faraci FM, Didion SP |title=Vascular protection: superoxide dismutase isoforms in the vessel wall. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1367–73 |year= 2005 |pmid= 15166009 |doi= 10.1161/01.ATV.0000133604.20182.cf
*cite journal | author=Adachi T, Ohta H, Yamada H, "et al." |title=Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody. |journal=Clin. Chim. Acta |volume=212 |issue= 3 |pages= 89–102 |year= 1993 |pmid= 1477980 |doi=
*cite journal | author=Adachi T, Ohta H, Hayashi K, "et al." |title=The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro. |journal=Free Radic. Biol. Med. |volume=13 |issue= 3 |pages= 205–10 |year= 1992 |pmid= 1505778 |doi=
*cite journal | author=Marklund SL |title=Expression of extracellular superoxide dismutase by human cell lines. |journal=Biochem. J. |volume=266 |issue= 1 |pages= 213–9 |year= 1990 |pmid= 2106874 |doi=
*cite journal | author=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 |year= 1991 |pmid= 2276747 |doi=
*cite journal | author=Hjalmarsson K, Marklund SL, Engström A, Edlund T |title=Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 18 |pages= 6340–4 |year= 1987 |pmid= 3476950 |doi=
*cite journal | author=Marklund SL |title=Extracellular superoxide dismutase in human tissues and human cell lines. |journal=J. Clin. Invest. |volume=74 |issue= 4 |pages= 1398–403 |year= 1984 |pmid= 6541229 |doi=
*cite journal | author=Yamada H, Yamada Y, Adachi T, "et al." |title=Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum. |journal=Jpn. J. Hum. Genet. |volume=40 |issue= 2 |pages= 177–84 |year= 1995 |pmid= 7662997 |doi=
*cite journal | author=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 |year= 1994 |pmid= 7959763 |doi= 10.1006/geno.1994.1357
*cite journal | author=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=J. Biol. Chem. |volume=269 |issue= 29 |pages= 19163–6 |year= 1994 |pmid= 8034674 |doi=
*cite journal | author=Adachi T, Yamada H, Yamada Y, "et al." |title=Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface. |journal=Biochem. J. |volume=313 ( Pt 1) |issue= |pages= 235–9 |year= 1996 |pmid= 8546689 |doi=
*cite journal | author=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=Biochem. J. |volume=317 ( Pt 1) |issue= |pages= 51–7 |year= 1996 |pmid= 8694786 |doi=
*cite journal | author=Adachi T, Morihara N, Yamazaki N, "et al." |title=An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases. |journal=J. Biochem. |volume=120 |issue= 1 |pages= 184–8 |year= 1997 |pmid= 8864862 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Enghild JJ, Thogersen IB, Oury TD, "et al." |title=The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 14818–22 |year= 1999 |pmid= 10329680 |doi=
*cite journal | author=Bowler RP, Nicks M, Olsen DA, "et al." |title=Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16505–11 |year= 2002 |pmid= 11861638 |doi= 10.1074/jbc.M105409200
*cite journal | author=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 |year= 2002 |pmid= 12052468 |doi=
*cite journal | author=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=J. Biol. Chem. |volume=278 |issue= 9 |pages= 6824–30 |year= 2003 |pmid= 12475988 |doi= 10.1074/jbc.M207939200

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