Phosphorylation of rat liver glycogen synthase bound to the glycogen particle

1984 ◽  
Vol 235 (1) ◽  
pp. 186-195 ◽  
Author(s):  
Akira Akatsuka ◽  
Toolsee J. Singh ◽  
Kuo-Ping Huang
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Glycogen Particle

scholarly journals Regulation of rat liver glycogen synthase. Roles of Ca2+, phosphorylase kinase, and phosphorylase a.

1983 ◽  
Vol 258 (9) ◽  
pp. 5490-5497
Author(s):  
W G Strickland ◽  
M Imazu ◽  
T D Chrisman ◽  
J H Exton
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Phosphorylase Kinase

In vivo phosphorylation of liver glycogen synthase. Effect of glucose and glucagon treatment of liver cells on the distribution of the [32P] phosphate

1993 ◽  
Vol 71 (1-2) ◽  
pp. 90-96 ◽  
Author(s):  
Agnes W. H. Tan ◽  
Frank Q. Nuttall
Keyword(s):  
High Pressure ◽  
Liquid Chromatography ◽  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Liver Cells ◽  
Phosphorylation State ◽  
Glucose Treatment ◽  
Effect Of Glucose

Glycogen synthase was phosphorylated in vivo by perfusing rat liver or incubating liver cells with [32P]phosphate. It was then isolated by immunoprecipitation and subjected to exhaustive tryptic proteolysis. The trypsin-derived [32P]phosphopeptides were separated by high pressure liquid chromatography (HPLC). Incubation of in vivo phosphorylated synthase with endogenous synthase phosphatase to convert synthase D to synthase R resulted in removal of phosphate from all of the labeled phosphopeptides. In prelabeled liver cells treated with glucagon or glucose, the activities of synthase and phosphorylase changed in the direction expected. The total labeling in the immunoprecipitated synthase was found to be increased to 126% and decreased to 67% of the control with glucagon and glucose treatment, respectively. When the HPLC [32P]phosphopeptide profile of synthase from glucagon-treated animals was compared with that of controls, there were only minor differences in the two profiles. All the peaks were present and the proportion of labeling in each remained similar. There also was only a modest change in the [32P]phosphopeptide profile with glucose treatment when compared with that of controls. These results indicate that regulation of synthase activity in the hepatocyte involves changes in phosphorylation at multiple sites. Indeed, in 32P-labeled liver cells, all of the labeled sites appeared to be involved.Key words: glycogen synthase, liver, phosphorylation state, glucose treatment, glucagon treatment.

Role of protein kinase C in the regulation of rat liver glycogen synthase

1987 ◽  
Vol 252 (1) ◽  
pp. 81-90 ◽  
Author(s):  
Hiroki Nakabayashi ◽  
Kai-Foon Jesse Chan ◽  
Kuo-Ping Huang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Kinase C

scholarly journals Phosphorylation of rat liver glycogen synthase by phosphorylase kinase.

1984 ◽  
Vol 259 (12) ◽  
pp. 7878-7883 ◽  
Author(s):  
A Akatsuka ◽  
T J Singh ◽  
K P Huang
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Phosphorylase Kinase

scholarly journals Glucagon-stimulated phosphorylation of rat liver glycogen synthase in isolated hepatocytes.

1985 ◽  
Vol 260 (6) ◽  
pp. 3239-3242
Author(s):  
A Akatsuka ◽  
T J Singh ◽  
H Nakabayashi ◽  
M C Lin ◽  
K P Huang
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Isolated Hepatocytes

Multiple phosphorylation sites of rat liver glycogen synthase

1986 ◽  
Vol 888 (2) ◽  
pp. 225-236 ◽  
Author(s):  
Yuhuan Wang ◽  
Marcella Camici ◽  
Fook-Thean Lee ◽  
Zafeer Ahmad ◽  
Anna A. DePaoli-Roach ◽  
...  
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Phosphorylation Sites
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