Selenoprotein P is a protein that in humans is encoded by the SEPP1 gene.[5][6]
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This gene encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 10 Sec residues (human, rat, mouse)[7] per polypeptide, one located at the C-terminal side of protein and others at the N-terminal side. It is a heparin-binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene.[6]
Mice and dogs with knock-out variants in their SEPP1 homologues (Selenop[8] and SELENOP[9] respectively) may develop cerebellar ataxia phenotypes.[10][11] SEPP1 and neural precursor cell levels in mouse brains increase post-exercise. Mice engineered to lack SEPP1 did not increase neural precursors.[12][13]
- Burk RF, Hill KE (October 1994). "Selenoprotein P. A selenium-rich extracellular glycoprotein". The Journal of Nutrition. 124 (10): 1891–1897. doi:10.1093/jn/124.10.1891. PMID 7931697.
- Mostert V (April 2000). "Selenoprotein P: properties, functions, and regulation". Archives of Biochemistry and Biophysics. 376 (2): 433–438. doi:10.1006/abbi.2000.1735. PMID 10775431.
- Hill KE, Lloyd RS, Yang JG, Read R, Burk RF (June 1991). "The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame". The Journal of Biological Chemistry. 266 (16): 10050–10053. doi:10.1016/S0021-9258(18)99185-4. PMID 2037562.
- Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Akesson B, Bellew T, Burk RF (February 1994). "Purification of selenoprotein P from human plasma". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1204 (2): 243–249. doi:10.1016/0167-4838(94)90014-0. PMID 8142465.
- Hill KE, Dasouki M, Phillips JA, Burk RF (September 1996). "Human selenoprotein P gene maps to 5q31". Genomics. 36 (3): 550–551. doi:10.1006/geno.1996.0505. PMID 8884283.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Mostert V, Lombeck I, Abel J (September 1998). "A novel method for the purification of selenoprotein P from human plasma". Archives of Biochemistry and Biophysics. 357 (2): 326–330. doi:10.1006/abbi.1998.0809. PMID 9735174.
- Saito Y, Hayashi T, Tanaka A, Watanabe Y, Suzuki M, Saito E, et al. (January 1999). "Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein p". The Journal of Biological Chemistry. 274 (5): 2866–2871. doi:10.1074/jbc.274.5.2866. PMID 9915822.
- Koyama H, Omura K, Ejima A, Kasanuma Y, Watanabe C, Satoh H (February 1999). "Separation of selenium-containing proteins in human and mouse plasma using tandem high-performance liquid chromatography columns coupled with inductively coupled plasma-mass spectrometry". Analytical Biochemistry. 267 (1): 84–91. doi:10.1006/abio.1998.2949. PMID 9918658.
- Arteel GE, Franken S, Kappler J, Sies H (March 2000). "Binding of selenoprotein P to heparin: characterization with surface plasmon resonance". Biological Chemistry. 381 (3): 265–268. doi:10.1515/BC.2000.034. PMID 10782998. S2CID 36448244.
- Hondal RJ, Ma S, Caprioli RM, Hill KE, Burk RF (May 2001). "Heparin-binding histidine and lysine residues of rat selenoprotein P". The Journal of Biological Chemistry. 276 (19): 15823–15831. doi:10.1074/jbc.M010405200. PMID 11278668.
- Nishimura K, Matsumiya K, Tsujimura A, Koga M, Kitamura M, Okuyama A (2001). "Association of selenoprotein P with testosterone production in cultured Leydig cells". Archives of Andrology. 47 (1): 67–76. doi:10.1080/01485010152104026 (inactive 2024-04-13). PMID 11442337.
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- Al-Taie OH, Seufert J, Mörk H, Treis H, Mentrup B, Thalheimer A, et al. (September 2002). "A complex DNA-repeat structure within the Selenoprotein P promoter contains a functionally relevant polymorphism and is genetically unstable under conditions of mismatch repair deficiency". European Journal of Human Genetics. 10 (9): 499–504. doi:10.1038/sj.ejhg.5200811. PMID 12173025.
- Saito Y, Takahashi K (November 2002). "Characterization of selenoprotein P as a selenium supply protein". European Journal of Biochemistry. 269 (22): 5746–5751. doi:10.1046/j.1432-1033.2002.03298.x. PMID 12423375.