scholarly journals Control of Liver Glycogen Synthase Activity and Intracellular Distribution by Phosphorylation

2009 ◽  
Vol 284 (10) ◽  
pp. 6370-6378 ◽  
Author(s):  
Susana Ros ◽  
Mar García-Rocha ◽  
Jorge Domínguez ◽  
Juan C. Ferrer ◽  
Joan J. Guinovart
1976 ◽  
Vol 231 (4) ◽  
pp. 1285-1289 ◽  
Author(s):  
O Giger ◽  
RE McCallum

The present study was undertaken to characterize endotoxin-induced changes in carbohydrate metabolism and more specifically, to determine the contribution of glycogenolysis to the loss of liver glycogen. Female ICR mice, fasted overnight, were injected with a median lethal dose (LD50, 9 mg/kg) of endotoxin extracted from Salmonella typhimurium strain SR-11. Glycogen synthase and glycogen phosphorylase activities were measured at 0.5 and 6 h after treatment. Endotoxin treatment did not alter total glycogen synthase activity, but the amount of enzyme present in the active form was significantly lower in endotoxic mice. There was no significant increase in glycogen phosphorylase activity in endotoxin-treated mice. Glycogen phosphorylase was activated to the same extent in control and endotoxic mice by decapitation or intravenous epinephrine (25 or 1 mug/kg). The results of this study indicate no significant increase in glycogen phosphorylase activity in endotoxic mice, contraindicating enhanced glycogenolysis as a mechanism for depletion of carbohydrate following endotoxin injection. Altered activation of glycogen synthase, however, may contribute to the loss of glycogen during endotoxemia.


2001 ◽  
Vol 357 (1) ◽  
pp. 17-24 ◽  
Author(s):  
Mar GARCÍA-ROCHA ◽  
Angela ROCA ◽  
Núria de la IGLESIA ◽  
Otto BABA ◽  
Josep M. FERNÁNDEZ-NOVELL ◽  
...  

Changes in the intracellular distribution of liver glycogen synthase (GS) might constitute a new regulatory mechanism for the activity of this enzyme at cellular level. Our previous studies indicated that incubation of isolated hepatocytes with glucose activated GS and resulted in its translocation from a homogeneous cytosolic distribution to the cell periphery. These studies also suggested a relationship with insoluble elements of the cytoskeleton, in particular actin. Here we show the translocation of GS in a different experimental model that allows the analysis of this phenomenon in long-term studies. We describe the reversibility of translocation of GS and its effect on glycogen distribution. Incubation of cultured rat hepatocytes with glucose activated GS and triggered its translocation to the hepatocyte periphery. The relative amount of the enzyme concentrated near the plasma membrane increased with time up to 8h of incubation with glucose, when the glycogen stores reached their maximal value. The lithium-induced covalent activation of GS was not sufficient to cause its translocation to the cell periphery. The intracellular distribution of GS closely resembled that of glycogen. Our results showed an interaction between GS and an insoluble element of the hepatocyte matrix. Although no co-localization between actin filaments and GS was observed in any condition, disruption of actin cytoskeleton resulted in a significantly lower percentage of cells in which the enzyme translocated to the cell periphery in response to glucose. This observation suggests that the microfilament network has a role in the translocation of GS.


Metabolism ◽  
1995 ◽  
Vol 44 (12) ◽  
pp. 1626-1630 ◽  
Author(s):  
I. Inoue ◽  
K. Takahashi ◽  
S. Katayama ◽  
Y. Harada ◽  
K. Negishi ◽  
...  

Author(s):  
John E. Michaels ◽  
Robert R. Cardell

Glycogen synthase (GS) is the rate limiting enzyme for liver glycogen synthesis and its activity varies with the phosphorylation state of the enzyme. The current study focused on changes in the intralobular patterns of distribution of cytochemically localized GS activity during glycogen synthesis.Normal and adrenalectomized (ADX) rats were fasted overnight to reduce liver glycogen to minimal levels. Fasted ADX rats received 2 mg dexamethasone (DEX) 0-8 h prior to sacrifice to stimulate glycogen synthesis. Liver was removed, rapidly frozen in isopentane cooled in liquid nitrogen, then cryostat sectioned. GS activity was localized histochemically by 3 h incubation in medium containing both UDP-glucose and glucose 6-phosphate. Glycogen was formed as reaction product. Control incubations omitted the substrate. Two stains were used to identify glycogen: 1) iodine staining of the incubated sections was rather specific for the newly formed glycogen (Figs. 1-6), whereas 2) periodic acid-Schiff (PAS) stained both native and nascent glycogen.


PEDIATRICS ◽  
2001 ◽  
Vol 108 (2) ◽  
pp. 495-497 ◽  
Author(s):  
S. L. Rutledge ◽  
J. Atchison ◽  
N. U. Bosshard ◽  
B. Steinmann

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