Abstract
Selenoprotein P (SeP) is a selenium-rich extracellular glycoprotein and is the major selenoprotein in plasma. SeP is presumed to be composed of two domains: one possesses redox-enzyme activity containing one selenocysteine residue in the N-terminal region, and the other functions as a selenium supplier containing nine selenocysteine residues in the C-terminal region. These domains are connected by a bridge containing two histidine-rich regions. Although the relationship between structure and function is not clear, SeP is reported to function as a peroxynitrite scavenger, or cell survival factor in the primary culture of neurons. Thus, SeP is a multifunctional protein. Increasing evidence indicates that SeP plays a significant role in vivo in the maintenance of selenium levels in the brain and testis. In the present review, we describe the structural properties and molecular function of SeP and discuss its significant role in cellular homeostasis, particularly in relation to selenium levels and the antioxidative system.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Hatfield DL, Berry MJ, Gladyshev VN (2006) Selenium: Its Molecular Biology and Role in Human Health. Springer-Verlag, New York
Squires JE, Berry MJ (2008) IUBMB life 60: 232
Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN (2003) Science 300: 1439
Motsenbocker MA, Tappel AL (1982) Biochimica et Biophysica Acta 719: 147
Burk RF (1973) Proc Soc Exp Biol Med 143: 719
Rotruck JT, Pope AL, Ganther HE, Swanson AB, Hafeman DG, Hoekstra WG (1973) Science 179: 588
Burk RF, Hill KE (2005) Ann Rev Nutr 25: 215
Burk RF, Hill KE (2009) Biochim Biophys Acta 1790: 1441
Hill KE, Lloyd RS, Burk RF (1993) Proc Nat Acad Sci USA 90: 537
Saito Y, Takahashi K (2000) J Health Sci 46: 409
Lu J, Holmgren A (2009) J Biol Chem 284: 723
Deagen JT, Butler JA, Zachara BA, Whanger PD (1993) Anal Biochem 208: 176
Burk RF, Hill KE, Boeglin ME, Ebner FF, Chittum HS (1997) Histochem Cell Biol 108: 11
Hondal RJ, Ma S, Caprioli RM, Hill KE, Burk RF (2001) J Biol Chem 276: 15823
Karlsson K, Lindahl U, Marklund SL (1988) Biochem J 256: 29
Karlsson K, Marklund SL (1988) Biochem J 255: 223
Hamer DH (1986) Ann Rev Biochem 55: 913
Saito Y, Hayashi T, Tanaka A, Watanabe Y, Suzuki M, Saito E, Takahashi K (1999) J Biol Chem 274: 2866
Suzuki KT, Sasakura C, Yoneda S (1998) Biochim Biophys Acta 1429: 102
Yoneda S, Suzuki KT (1997) Toxicol Appl Pharmacol 143: 274
Kaneko JJ, Ralston NV (2007) Biol Trace Elem Res 119: 242
Himeno S, Chittum HS, Burk RF (1996) J Biol Chem 271: 15769
Ma S, Capriolia RM, Hill KE, Burk RF (2003) J Am Soc Mass Spectrom 14: 593
Akesson B, Bellew T, Burk RF (1994) Biochim Biophys Acta 1204: 243
Yang JG, Morrison-Plummer J, Burk RF (1987) J BiolChem 262: 13372
Saito Y, Sato N, Hirashima M, Takebe G, Nagasawa S, Takahashi K (2004) Biochem J 381: 841
Kato H, Nagasawa S, Iwanaga S (1981) Methods Enzymol 80: 172
Cochrane CG, Revak SD, Wuepper KD (1973) J Exp Med 138: 1564
Mandle RJ, Kaplan AP (1977) J Biol Chem 252: 6097
Ma S, Hill KE, Caprioli RM, Burk RF (2002) J Biol Chem 277: 12749
Kryukov GV, Gladyshev VN (2000) Genes Cells 5: 1049
Takebe G, Yarimizu J, Saito Y, Hayashi T, Nakamura H, Yodoi J, Nagasawa S, Takahashi K (2002) J Biol Chem 277: 41254
Saito Y, Takahashi K (2002) Eur J Biochem/FEBS 269: 5746
Sies H, Arteel GE (2000) Free Rad Biol Med 28: 1451
Yamamoto Y, Takahashi K (1993) Arch Biochem Biophys 305: 541
Kernstock RM, Girotti AW (2008) Prot Exp Purificat 62: 216
Saito Y, Yoshida Y, Akazawa T, Takahashi K, Niki E (2003) J Biol Chem 278: 39428
Saito Y, Yoshida Y, Niki E (2007) FEBS lett 581: 4349
Ursini F, Maiorino M, Gregolin C (1985) Biochim Biophys Acta 839: 62
Masutani H, Yodoi J (2002) Methods Enzymol 347: 279
Wakasugi N, Tagaya Y, Wakasugi H, Mitsui A, Maeda M, Yodoi J, Tursz T (1990) Proc Nat Acad Sci USA 87: 8282
Soderberg A, Sahaf B, Rosen A (2000) Cancer Res 60: 2281
McKeehan WL, Hamilton WG, Ham RG (1976) Proc Nat Acad Sci USA 73: 2023
Thomas JP, Maiorino M, Ursini F, Girotti AW (1990) J Biol Chem 265: 454
Yan J, Barrett JN (1998) J Neurosci 18: 8682
Steinbrenner H, Bilgic E, Alili L, Sies H, Brenneisen P (2006) Free Rad Res 40: 936
Bosschaerts T, Guilliams M, Noel W, Herin M, Burk RF, Hill KE, Brys L, Raes G, Ghassabeh GH, De Baetselier P, Beschin A (2008) J Immunol 180: 6168
Valentine WM, Abel TW, Hill KE, Austin LM, Burk RF (2008) J Neuropath Exp Neurol 67: 68
Yoshida Y, Itoh N, Hayakawa M, Habuchi Y, Saito Y, Tsukamoto Y, Cynshi O, Jishage KI, Arai H, Niki E (2010) J Nutr Biochem 21: 66
Schweizer U, Streckfuss F, Pelt P, Carlson BA, Hatfield DL, Kohrle J, Schomburg L (2005) Biochem J 386: 221
Scharpf M, Schweizer U, Arzberger T, Roggendorf W, Schomburg L, Kohrle J (2007) J Neural Transm 114: 877
Bellinger FP, He QP, Bellinger MT, Lin Y, Raman AV, White LR, Berry MJ (2008) J Alzheimers Dis 15: 465
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2011 Zhejiang University Press, Hangzhou and Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Saito, Y., Takahashi, K. (2011). Selenoprotein P. In: Selenoproteins and Mimics. Advanced Topics in Science and Technology in China. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-22236-8_5
Download citation
DOI: https://doi.org/10.1007/978-3-642-22236-8_5
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-22235-1
Online ISBN: 978-3-642-22236-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)