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SEPP1  -  selenoprotein P, plasma, 1

Homo sapiens

Synonyms: SELP, SeP, Selenoprotein P
 
 
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Disease relevance of SEPP1

  • Previously, we have demonstrated dramatically reduced SeP expression in human colon adenomas [1].
  • An association of SeP with the vascular endothelium, a prime target of peroxynitrite toxicity, was shown in vivo [2].
  • We show that primary human astrocytes and the human astrocytoma cell line MOG-G-CCM express SeP as an unglycosylated protein, which is not secreted [3].
  • Spodoptera frugiperda insect cells (IPLB-Sf21-AE) (Sf21), infected with baculovirus expression vectors during their exponential growth phase, are commonly used to produce a variety of heterologous recombinant proteins [4].
  • Our data on the inhibition of selenoprotein synthesis and on repression of SeP promoter activity show that the expression of selenoproteins, especially of SeP, is influenced by acute phase reaction and pro-inflammatory reactions [5].
 

High impact information on SEPP1

  • SeP expression in astrocytes is constitutive [3].
  • Furthermore, specific downregulation of SeP expression by small interfering RNA decreases cell viability of human astrocytes and makes them more susceptible to t-BHP-induced cytotoxicity [3].
  • Preincubation of astrocytes with hepatocyte-derived SeP mimicks the protective effect of low-molecular-weight selenocompounds such as sodium selenite or selenomethionine against oxidative damage, shielding astrocytes from t-BHP-induced cytotoxicity [3].
  • Our results implicate an antioxidant activity of constitutively expressed SeP in selenium-deficient astrocytes, while during adequate selenium supply the enhanced protection against oxidative stress is exerted by cGPx [3].
  • SeP in human plasma protects against peroxynitrite-mediated oxidation and reduces phospholipid hydroperoxide in vitro, in accordance with the presumption that it has a function as an extracellular oxidant defense [6].
 

Biological context of SEPP1

 

Anatomical context of SEPP1

  • SeP is expressed in the gastrointestinal tract and the liver, where its expression is downregulated by various proinflammatory cytokines (Il1beta, TGFbeta, IFNgamma) [1].
  • SeP binds to heparin and cell membranes, and is associated with endothelial cells [6].
  • The effect of cytokines on the expression of selenoprotein P (SeP) in the human liver cell line HepG2 was investigated [9].
  • Because SeP associates with endothelial membranes, it may act in vivo as a protective factor inhibiting the oxidation of LDL by reactive oxygen species [7].
  • A major fraction of the essential trace element selenium circulating in human blood plasma is present as selenoprotein P (SeP) [8].
 

Associations of SEPP1 with chemical compounds

 

Analytical, diagnostic and therapeutic context of SEPP1

  • SeP of bovine serum acts as a survival-promoting factor in neuronal cell culture [2].
  • RT-PCR analysis of SeP mRNA expression demonstrated an inhibition of SeP transcription to 40+/-2% of control levels after 24 h [9].
  • Conversely, Western analysis revealed a dose-dependent reduction of SeP content in culture medium after treatment with transforming growth factor (TGF)-beta1 with an 1C50 of 31 pM [9].
  • The latter was used for further batch and continuous cultivation of Sf21 cells in a perfused 1.4-l stirred-tank bioreactor with special attention to the oxygen requirement of these cells [4].

References

  1. 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. Al-Taie, O.H., Seufert, J., Mörk, H., Treis, H., Mentrup, B., Thalheimer, A., Starostik, P., Abel, J., Scheurlen, M., Köhrle, J., Jakob, F. Eur. J. Hum. Genet. (2002) [Pubmed]
  2. Selenoprotein P: properties, functions, and regulation. Mostert, V. Arch. Biochem. Biophys. (2000) [Pubmed]
  3. Involvement of selenoprotein P in protection of human astrocytes from oxidative damage. Steinbrenner, H., Alili, L., Bilgic, E., Sies, H., Brenneisen, P. Free Radic. Biol. Med. (2006) [Pubmed]
  4. Optimization of the growth conditions of Sf21 insect cells for high-density perfusion culture in stirred-tank bioreactors. Deutschmann, S.M., Jäger, V. Enzyme Microb. Technol. (1994) [Pubmed]
  5. The influence of the cytokines Il-1beta and INFgamma on the expression of selenoproteins in the human hepatocarcinoma cell line HepG2. Hesse-Bähr, K., Dreher, I., Köhrle, J. Biofactors (2000) [Pubmed]
  6. Selenoprotein P. Moschos, M.P. Cell. Mol. Life Sci. (2000) [Pubmed]
  7. Selenoprotein P protects low-density lipoprotein against oxidation. Traulsen, H., Steinbrenner, H., Buchczyk, D.P., Klotz, L.O., Sies, H. Free Radic. Res. (2004) [Pubmed]
  8. Selenoprotein P protects endothelial cells from oxidative damage by stimulation of glutathione peroxidase expression and activity. Steinbrenner, H., Bilgic, E., Alili, L., Sies, H., Brenneisen, P. Free Radic. Res. (2006) [Pubmed]
  9. Transforming growth factor-beta1 inhibits expression of selenoprotein P in cultured human liver cells. Mostert, V., Dreher, I., Kohrle, J., Abel, J. FEBS Lett. (1999) [Pubmed]
  10. Genistein affects androgen-responsive genes through both androgen- and estrogen-induced signaling pathways. Takahashi, Y., Hursting, S.D., Perkins, S.N., Wang, T.C., Wang, T.T. Mol. Carcinog. (2006) [Pubmed]
 
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