Abstract
Selenoprotein P can be traced to reports in the early 1970s that demonstrated 75Se incorporation into a plasma protein in the rat (Millar, 1972; Burk, 1973). Later Herrman (1977) showed that this plasma protein was distinct from glutathione peroxidase. It was referred to as selenoprotein P by Tappel’s group because of its plasma location (Motsenbocker and Tappel, 1982) and as 75Se-P by our group because of its incorporation of 75Se (Burk and Gregory, 1982). All workers have now adopted the name of selenoprotein P because it has been shown to be a selenoprotein and it is present in plasma. A further name change will be necessary when its function is established.
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References
Berry, MJ, Banu, L, Chen, Y, Mandel, SJ, Kieffer, JD, Harney, JW, Larsen, PR. Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3’ untranslated region. Nature 353:273 – 276; 1991a.
Berry, MJ, Banu, L, Larsen, PR. Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature 349:438 – 440; 1991b.
Böck, A. Incorporation of selenium into bacterial selenoproteins. In:Burk, RF, ed. Selenium in Biology and Human Health. New York:Springer Verlag; 1993.
Burk, RF. Effect of dietary selenium on 75Se binding to rat plasma proteins. Proc Soc Exp Biol Med 143:719 – 722; 1973.
Burk, RF, Gregory, PE. Some characteristics of 75Se-P, a selenoprotein found in rat liver and plasma, and comparison of it with selenoglutathione peroxidase. Arch Biochem Biophys 213:78 – 80; 1982.
Burk, RF, Hill, KE, Read, R, Bellew, T. Response of rat selenoprotein P to selenium administration and fate of its selenium Am J Physiol 261:E26 - E30; 1991.
Burk, RF, Lawrence, RA, Lane, JM. Liver necrosis and lipid peroxidation in the rat as the result of paraquat and diquat administration. J Clin Invest 65:1024 - 1031; 1980.
Gomez, B, Tappel, AL. Selenoprotein P receptor from rat. Biochim Biophys Acta 979:20 - 26; 1989.
Herrman, JL. The properties of a rat serum protein labelled by the injection of sodium selenite. Biochim Biophys Acta 500:61 - 70; 1977.
Hill, KE, Lloyd, RS, Burk, RF. Conserved nucleotide sequences in the open reading frame and 3’ untranslated region of selenoprotein P mRNA. Proc Natl Acad Sci USA 90:537 - 541, 1993.
Hill, KE, Lloyd, RS, Yang, JG, Read, R, Burk, RF. The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame. J Biol Chem 266:10050 - 10053; 1991.
Hill, KE, Lyons, PR, Burk, RF. Differential regulation of rat liver selenoprotein mRNAs in selenium deficiency. Biochem Biophys Res Commun 185:260 – 263; 1992.
Kato, T, Read, R, Rozga, J, Burk, RF. Evidence for intestinal release of absorbed selenium in a form with high hepatic extraction. Am J Physiol 262:G854-G858; 1992.
Millar, KR. Distribution of 75Se in liver, kidney, and blood proteins of rats after intravenous injection of sodium selenite. NZJ Agr Res 15:547–564; 1972.
Motchnik, PA, Tappel, AL. Rat plasma selenoprotein P properties and purification. Biochim Biophys Acta 993:27 – 35; 1989.
Motsenbocker, MA, Tappel, AL. A selenocysteine-containing selenium- transport protein in rat plasma. Biochim Biophys Acta 719:147–153; 1982.
Read, R, Bellew, T, Yang, JG, Hill, KE, Palmer, IS, Burk, RF. Selenium and amino acid composition of selenoprotein P, the major selenoprotein in rat serum. J Biol Chem 265:17899 - 17905; 1990.
Saedi, MS, Smith, CG, Frampton, J, Chambers, I, Harrison, PR, Sunde, RA. Effect of selenium status on mRNA levels for glutathione peroxidase in rat liver. Biochem Biophys Res Commun 153:855 - 861; 1988.
Yang, JG, Hill, KE, Burk, RF. Dietary selenium intake controls rat plasma selenoprotein P concentration. J Nutr 119:1010 - 1012; 1989.
Yang, JG, Morrison-Plummer, J, Burk, RF. Purification and quantitation of a rat plasma selenoprotein distinct from glutathione peroxidase using monoclonal antibodies. J Biol Chem 262:13372 - 13375; 1987.
Zinoni, F, Heider, J, Böck, A. Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine. Proc Natl Acad Sci USA 87:4660 - 4664; 1990.
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© 1994 Springer-Verlag New York
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Hill, K.E., Burk, R.F. (1994). Selenoprotein P—An Extracellular Protein Containing Multiple Selenocysteines. In: Burk, R.F. (eds) Selenium in Biology and Human Health. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2592-8_7
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DOI: https://doi.org/10.1007/978-1-4612-2592-8_7
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