Selenoprotein P is a protein that in humans is encoded by the SEPP1gene.[5][6]
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]
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. PMID10775431.
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. PMID8125298.
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. PMID8142465.
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. PMID8884283.
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. PMID9373149.
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. PMID9735174.
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. PMID9918658.
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. PMID10782998. S2CID36448244.
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). PMID11442337.{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (link)
