Hormonal Influence on Sex Hormone Binding Protein (SHBP) Production by HEP G2 Cells

1989 ◽  
Vol 76 (s20) ◽  
pp. 14P-15P
Author(s):  
AP Stubbs ◽  
SEJ Edmunds ◽  
AA Santos ◽  
ML Wilkinson
Keyword(s):  
Binding Protein ◽  
Sex Hormone ◽  
Hormone Binding ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Hormonal Influence ◽  
Hormone Binding Protein ◽  
G2 Cells

Regulation of Sex Hormone Binding Globulin (SHBG) production in hep G2 cells by insulin

Steroids ◽  
1988 ◽  
Vol 52 (4) ◽  
pp. 339-340 ◽  
Author(s):  
S.R. Plymate ◽  
R.E. Jones ◽  
L.A. Matej ◽  
K.E. Friedl
Keyword(s):  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
G2 Cells

Sex hormone–binding protein: biomarker and hepatokine?

2021 ◽  
Author(s):  
Pomme I.H.G. Simons ◽  
Olivier Valkenburg ◽  
Coen D.A. Stehouwer ◽  
Martijn C.G.J. Brouwers
Keyword(s):  
Binding Protein ◽  
Sex Hormone ◽  
Hormone Binding ◽  
Protein Biomarker ◽  
Hormone Binding Protein

Regulation of IGF binding protein-1 in Hep G2 cells by cytokines and reactive oxygen species

1999 ◽  
Vol 276 (3) ◽  
pp. G719-G727 ◽  
Author(s):  
Charles H. Lang ◽  
Gerald J. Nystrom ◽  
Robert A. Frost
Keyword(s):  
Reactive Oxygen Species ◽  
Nuclear Translocation ◽  
Binding Protein ◽  
Reactive Oxygen ◽  
Free Radical Scavengers ◽  
Oxygen Species ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Tnf Α ◽  
G2 Cells

The liver is a major site of synthesis for insulin-like growth factor binding protein (IGFBP)-1. Because IGFBP-1 inhibits many anabolic actions of IGF-I, increases in IGFBP-1 may be partly responsible for the decrease in lean body mass observed in catabolic/inflammatory conditions. This study aimed to determine in Hep G2 cells 1) the sensitivity of IGFBP-1 synthesis to treatment with interleukin (IL)-1, tumor necrosis factor-α (TNF-α), and IL-6, 2) the ability of reactive oxygen species (ROS) to enhance IGFBP-1 production, and 3) the role of ROS in mediating cytokine-induced increases in IGFBP-1. Hep G2 cells responded to IL-1β, TNF-α, and IL-6 with maximal 8- to 10-fold increases in IGFBP-1 production. Although the maximal responsiveness of cells treated with TNF-α and IL-6 was 20–30% less than that with IL-1β, cells demonstrated a similar sensitivity to all cytokines (half-maximal responsive dose of ∼10 ng/ml). A low concentration (3 ng/ml) of all three cytokines had an additive effect on IGFBP-1 production. Cytokines also increased IGFBP-1 mRNA. The half-life of IGFBP-1 mRNA was ∼4 h and not altered by IL-1β. Incubation with ROS, including H2O2and nitric oxide (NO) donors, resulted in a relatively smaller increase in IGFBP-1. However, preincubating Hep G2 cells with various free radical scavengers and NO synthase and eicosanoid inhibitors failed to prevent or attenuate cytokine-induced increases in IGFBP-1. Finally, preincubating cells with pyrrolidinedithiocarbamate (PDTC) but not SN50 (inhibitors of nuclear factor-κB activation and nuclear translocation, respectively) attenuated increases in IGFBP-1 induced by IL-1. These results indicate that 1) proinflammatory cytokines directly enhance IGFBP-1 synthesis by stimulating transcription without altering mRNA stability, 2) addition of exogenous ROS also stimulates IGFBP-1 production but to a smaller extent than cytokines, and 3) the cytokine-induced increase in IGFBP-1 production is not mediated by endogenous production of ROS or eicosanoids but appears to at least partially involve a PDTC-sensitive pathway.

Human Hepatoma (Hep G2) Cells Secrete a Novel T4-Binding Protein (27 K Protein)

1986 ◽  
pp. 477-480 ◽  
Author(s):  
Luigi Bartalena ◽  
Settimio Grimaldi ◽  
Jacob Robbins
Keyword(s):  
Binding Protein ◽  
Human Hepatoma ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
G2 Cells
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