Prostaglandin E2 stimulates synthesis of insulin-like growth factor binding protein-3 in rat bone cells in vitro

2009 ◽  
Vol 7 (10) ◽  
pp. 1157-1163 ◽  
Author(s):  
Christoph Schmid ◽  
Irene Schläpfer ◽  
Margaretha Waldvogel ◽  
Jürgen Zapf ◽  
E. Rudolf Froesch
Keyword(s):  
Growth Factor ◽  
Prostaglandin E2 ◽  
Bone Cells ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Rat Bone

INSULIN AND VARIATION IN GLUCOSE LEVELS MODIFY THE SECRETION RATES OF THE GROWTH HORMONE-INDEPENDENT INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN-1 IN THE HUMAN HEPATOBLASTOMA CELL LINE HEP G2

1989 ◽  
Vol 123 (3) ◽  
pp. R17-R20 ◽  
Author(s):  
A.M. Cotterill ◽  
C.T. Cowell ◽  
M. Silink
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Glucose Concentration ◽  
Binding Protein ◽  
Suitable Model ◽  
Insulin Like Growth Factor ◽  
Hep G2 ◽  
Factor Binding ◽  
Glucose Levels

ABSTRACT The plasma level of the GH-independent insulin-like growth factor binding-protein-1 (IGFBP-1) is regulated inversely by insulin. In this study the effect of insulin and changes in the glucose concentration on in-vitro IGFBP-1 secretion by the Hep G2 cell line was studied. Media from confluent cells in 12 replicates were collected for consecutive periods: initial control (20 h), study(6 h) and recovery (20 h). Insulin suppressed IGFBP-1 secretion maximally at 100 mU/1 (−32%) within 6 h. The secretion of IGFBP-1 was stimulated by a decrease in the glucose concentration in the medium, maximally (+25%) with a decrease from 24 to 6 mmol/l. Stimulation by varying glucose levels and suppression by insulin of IGFBP-1 secretion persisted on return to control conditions after the removal of physiological concentrations of glucose (4 - 12 mmol/l) and insulin (50 - 500 mU/1). The findings in the Hep G2 cell line that a variation in the physiological concentrations of glucose and insulin each independently regulate IGFBP-1 secretion suggest that this cell line may by a suitable model for further in-vitro studies of the regulation of secretion of IGFBP-1.

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