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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
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1437-4315
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Volume 388, Issue 10

Issues

Post-translational processing of selenoprotein P: implications of glycosylation for its utilisation by target cells

Holger Steinbrenner
  • 1Institute for Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
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/ Lirija Alili
  • 2Institute for Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Dominik Stuhlmann
  • 3Institute for Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Helmut Sies
  • 4Institute for Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Peter Brenneisen
  • 5Institute for Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-10-16 | DOI: https://doi.org/10.1515/BC.2007.136

Abstract

Selenoprotein P (SeP) is a highly glycosylated plasma protein containing up to 10 selenocysteine residues. It is secreted by hepatocytes and also by the human hepatoma cell line HepG2. Pharmacological inhibitors interfering with N-glycosylation, intracellular trafficking and calcium homeostasis were applied to examine post-translational processing and secretion of SeP by HepG2 cells. In parallel, the prototypic secretory glycoprotein α1-antitrypsin was used as technical control. Secretion of SeP was stimulated by increasing the extracellular calcium concentration and by inhibiting the release of sequestered calcium through dantrolene or U-73122. In contrast, brefeldin A and thapsigargin suppressed SeP secretion. Tunicamycin and monensin induced the synthesis of truncated non-glycosylated and partially glycosylated forms of SeP, which were secreted in spite of their impaired glycosylation. Both non-glycosylated and partially glycosylated SeP is utilised as selenium donor by target cells: impaired glycosylation affected neither the ability of SeP to induce the synthesis of the selenoenzyme cytosolic glutathione peroxidase nor its capacity to protect endothelial cells from oxidative stress.

Keywords: calcium; Ea.hy926 endothelial cell; glutathione peroxidase; monensin; selenium; tunicamycin

About the article

Corresponding author


Received: 2007-04-30

Accepted: 2007-07-23

Published Online: 2007-10-16

Published in Print: 2007-10-01


Citation Information: Biological Chemistry, Volume 388, Issue 10, Pages 1043–1051, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.136.

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