scholarly journals Epidermal-growth-factor stimulation of gluconeogenesis in isolated rat hepatocytes involves the inactivation of pyruvate kinase

1989 ◽  
Vol 258 (3) ◽  
pp. 935-935
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Pyruvate Kinase ◽  
Rat Hepatocytes ◽  
Epidermal Growth Factor Stimulation ◽  
Isolated Rat Hepatocytes ◽  
Epidermal Growth ◽  
Isolated Rat ◽  
Stimulation Of

The Effect of Epidermal Growth Factor (EGF) on Thyroid Function in the Sheep and in Isolated Rat Hepatocytes

1986 ◽  
pp. 359-363
Author(s):  
Jo M. Corcoran ◽  
Michael J. Waters ◽  
Jonathan Marks ◽  
Greg Jorgensen ◽  
Kay V. Waite ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Thyroid Function ◽  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Epidermal Growth ◽  
Isolated Rat

scholarly journals The early stimulation of glycolysis by epidermal growth factor in isolated rat hepatocytes is secondary to the glycogenolytic effect

1995 ◽  
Vol 308 (3) ◽  
pp. 889-894 ◽  
Author(s):  
I Quintana ◽  
M Grau ◽  
F Moreno ◽  
C Soler ◽  
I Ramírez ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Rat Hepatocytes ◽  
Rat Hepatocyte ◽  
Isolated Rat Hepatocytes ◽  
End Products ◽  
Glycogenolytic Effect ◽  
Free Glucose ◽  
Epidermal Growth ◽  
Stimulation Of

We have studied the relationship between the effect of epidermal growth factor (EGF) on glycogen metabolism and its effect on glycolysis, in rat hepatocyte suspensions. Although 10 nM glucagon or 10 microM adrenaline increased glycogen degradation by more than 120%, 10 nM EGF increased glycogenolysis by less than 20% in hepatocytes incubated in glucose-free medium. Both glucagon and adrenaline increased phosphorylase a activity by more than 130%; EGF increased this activity by about 30%. Under basal conditions, 65% of the glucosyl residues were released as free glucose and about 30% ended up as C3 molecules (lactate and pyruvate). Both glucagon and adrenaline decreased the proportion of glucosyl units that rendered glycolysis end-products (to 2% for glucagon and 6% for adrenaline) and increased the proportion that ended up as free glucose (to 94% and 88% of the glucosyl residues for glucagon and adrenaline respectively). EGF increased the production of both free glucose and lactate+pyruvate, but the proportion of glucosyl residues that ended up as free glucose or glycolysis end-products was unchanged. In glycogen-depleted hepatocytes incubated in the presence of 25 mM glucose, EGF affected neither glycogen deposition nor glycolysis. EGF increased cytosolic free Ca2+, and neomycin decreased both the Ca2+ signal and the glycogenolytic effect. In conclusion, our results indicate that the effect of EGF on glycolysis is secondary to the Ca(2+)-mediated stimulation of glycogenolysis in rat hepatocyte suspensions.

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