Hormonal effects on the secretion and glycoform profile of corticosteroid-binding globulin

Robin Mihrshahi*, John G. Lewis, Sinan O. Ali

*Corresponding author for this work

Research output: Contribution to journalArticle

20 Citations (Scopus)


Corticosteroid-binding globulin (CBG) is a plasma glycoprotein that is primarily synthesized in the liver and binds cortisol and progesterone with high affinity. In this study, a CBG secreting hepatocellular carcinoma derived cell line (HepG2) was used to investigate the hormonal regulation of hepatic CBG synthesis. HepG2 cells were grown for 72 h in 30, 300 and 3000 nM concentrations of estradiol (E 2), testosterone (T), insulin, thyroxin (T 4) and dexamethasone (DMZ) and the secreted CBG quantified by a novel enzyme-linked immunosorbent assay (ELISA). Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) was carried out to determine the effects of these hormones on the relative distribution of CBG glycoforms. Insulin, T 4 and high concentrations of E 2 decreased the secretion of CBG by HepG2 cells (p < 0.05). Ethanol, the solvent used for E 2, T and DMZ, also significantly attenuated CBG secretion. 2D-PAGE resolved 13-14 glycoforms of CBG produced by HepG2 cells. Insulin caused a reduction in the synthesis of more acidic, while T 4 and DMZ decreased the production of more basic CBG glycoforms. Stimulation with E 2 resulted in the synthesis of additional isoforms of increased acidity, which may represent a type of CBG only seen during pregnancy in vivo. Possible physiological implications of these findings are discussed.

Original languageEnglish
Pages (from-to)275-285
Number of pages11
JournalJournal of Steroid Biochemistry and Molecular Biology
Issue number4-5
Publication statusPublished - Nov 2006


  • Corticosteroid-binding globulin (CBG)
  • HepG2
  • Hormonal regulation
  • Two-dimensional polyacrylamide gel-electrophoresis

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