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PubMed1954

[Liver glycogen].

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Glycogen↗
PubMed1982

[Liver glycogen of the Wistar rat in experimental chronic cadmium intoxication under seasonal conditions].

Male Wistar-rats were used to investigate the liver glycogen pattern quantitatively under normal conditions and after oral application of CdCl2 (dosage: 50 ppm or 150 ppm) solved in drinking-water. The duration of the experiment was 1,3,6, or 12 month. The control animals have the lowest liver glycogen content at the beginning of the spring. During the summer, the liver glycogen content is increased and reached the highest level at the ending of the year. Under cadmium influence the liver glycogen content was diminished. The cadmium-effect is influenced by seasons. There is a small cadmium-effect in the time of a low liver glycogen content at the beginning of the spring. With the increasing liver glycogen content in the June, temporary the cadmium-effect is increasing too. The strongest cadmium-effect was obtained in the phase of the cadmium-effect is increasing too. The strongest cadmium-effect was obtained in the phase of high liver glycogen accumulation at the ending of the year.

Animals↗
PubMed1984

Phosphorylation of rabbit liver glycogen synthase by multiple protein kinases.

Purified rabbit liver glycogen synthase was found to be a substrate for six different protein kinases: (i) cyclic AMP-dependent protein kinase, (ii) two Ca2+-stimulated protein kinases, phosphorylase kinase (from muscle) and a calmodulin-dependent glycogen synthase kinase, and (iii) three members of a Ca2+ and cyclic nucleotide independent class, PC0.7, FA/GSK-3, and casein kinase-1. Greatest inactivation accompanied phosphorylation by cyclic AMP-dependent protein kinase (to 0.5-0.7 phosphate/subunit, +/- glucose-6-P activity ratio reduced from approximately 1 to 0.6) or FA/GSK-3 (to approximately 1 phosphate/subunit, activity ratio, 0.46). Phosphorylation by the combination FA/GSK-3 plus PC0.7 was synergistic, and more extensive inactivation was achieved. The phosphorylation reactions just described caused significant reductions in the Vmax of the glycogen synthase with little effect on the S0.5 (substrate concentration corresponding to Vmax/2). Phosphorylase kinase achieved a lesser inactivation, to an activity ratio of 0.75 at 0.6 phosphate/subunit. PC0.7 acting alone, casein kinase-1, and the calmodulin-dependent protein kinase did not cause inactivation of liver glycogen synthase with the conditions used. Analysis of CNBr fragments of phosphorylated glycogen synthase indicated that the phosphate was distributed primarily between two polypeptides, with apparent Mr = 12,300 (CB-I) and 16,000-17,000 (CB-II). PC0.7 and casein kinase-1 displayed a decided specificity for CB-II, and the calmodulin-dependent protein kinase was specific for CB-I. The other protein kinases were able, to some extent, to introduce phosphate into both CB-I and CB-II. Studies using limited proteolysis indicated that CB-II was located at a terminal region of the subunit. CB-I contains a minimum of one phosphorylation site and CB-II at least three sites. Liver glycogen synthase is therefore potentially subject to the same type of multisite regulation as skeletal muscle glycogen synthase although the muscle and liver enzymes display significant differences in both structural and kinetic properties.

Animals↗
PubMed1986

[Effect of ganglionectomy (superior cervical ganglia) at normal temperature and exposure to cold on the circadian rhythm of liver glycogen and blood glucose levels of the Wistar rat with regard to the pineal gland].

Liver glycogen content and blood glucose level of 80 male Wistar rats were measured 4 times a day, 30 d after following surgeries: sham-operation without exposure to cold, sham-operation with exposure to cold (283 K, 72 h before killing), extirpation of the ganglia cervicalia superiora (GX) without exposure to cold, extirpation of the ganglia cervicalia superiora with exposure to cold (283 K, 72 h before killing). Exposure to cold alone as well as GX with and without exposure to cold modify the unimodal daily patterns (curves were calculated by means of empirical regression) of liver glycogen content and blood glucose level: there are changes from contrary localization of the maxima (and minima) of both, liver glycogen content and blood glucose level (exposure to cold alone) to nearly equal localization (GX alone). Compared to control group, all surgeries reduce the liver glycogen content statistical-significantly and also enhance the blood glucose level. Combination of GX with exposure to cold shows the strongest effect. In this case, the influence of GX is visible, but the effect is not significantly different from this of exposure to cold alone, which causes a high activation of the metabolism. To the contrary, a statistically significant influence is to be seen after GX alone, but the effect is lower than this one of exposure to cold. Extirpation of the ganglia cervicalia superiora and the resulting sympathetic denervation of the pineal gland is answered by comparable reactions of the investigated parameters as the extirpation of the pineal gland itself (90 d post operationem). Diminuation of liver glycogen content and enhancement of blood glucose level characterize the influence of gangliectomy (30 d post operationem) in this way, that the ratio of effect of factors causing hypo- and hyperglycemia is changed in favour of the latter.

Animals↗
PubMed1990

Participation of calcium ion on depletion mechanism of liver glycogen by purified glucocorticoid antagonizing factor released in blood during endotoxemia.

The present study was conducted by the use of purified glucocorticoid antagonizing factor (GAF) released in blood of endotoxemic mice to determine whether or not the factor (GAF and Ca2+) may play a possible role of mediator in depletion mechanism of liver glycogen in endotoxemia. The liver glycogen level in 2 hr after injection with GAF plus cortisone-treated mice was markedly lower than that in cortisone alone-treated mice. However, the administration of trifluoperazine or verapamil markedly increased glycogen levels in liver of GAF plus cortisone-injected mice. On the other hand, when the mice fed a calcium-free diet were injected with GAF plus cortisone, there was merely a significant difference in liver glycogen level as compared to cortisone alone-treated mice. The level of Ca2+ in liver cytosol fraction in cortisone-treated mice was higher 2 hr after GAF injection than that in the cortisone alone-treated one. The phosphorylase a activity in liver 2 hr after injection of GAF plus cortisone did not show a significant difference as compared to that in mice treated with cortisone alone. However, the activity ratio of glycogen synthase enzyme (synthase I synthase I + D) was decreased in GAF plus cortisone-treated mice as compared to that in cortisone alone-treated mice. These findings suggest that there are participations of Ca2+ and mediator GAF released from reticuloendothelial system (RES macrophages in glucoregulation of endotoxemia. Thus, it may be speculated that intracellular Ca2+ may mediate glycogenesis rather than glycogenolysis in the depletion mechanism of liver glycogen during GAF-poisoning.

Animals↗
PubMed1987

Liver glycogen metabolism in endotoxin shock. II. Endotoxin administration increases glycogen phosphorylase activities in dog livers.

The effects of E. coli endotoxin administration on hepatic glycogen phosphorylase activities in dogs were investigated. Hepatic glycogen phosphorylase activities in both control and endotoxic dogs were inactivated spontaneously by preincubation of enzyme preparations at 25 degrees C. Total glycogen phosphorylase activity was not significantly altered during preincubation. The activity of glycogen phosphorylase a was increased by 83 and 80% at 1 and 2 hr postendotoxin, respectively, without preincubation; and by 203 and 133% at 1 and 2 hr postendotoxin, respectively, after 30 min preincubation. Without preincubation, the glycogen phosphorylase percentage a activity was increased from the control value of 37 to 58% at 1 hr postendotoxin and to 53% at 2 hr postendotoxin. After 30 min preincubation, the glycogen phosphorylase percentage a activity was increased from the control value of 10 to 28% at 1 hr postendotoxin and to 20% at 2 hr postendotoxin. The time required for half maximum inactivation of percentage a activity was 16.5, 33, and 24 min for control, 1 and 2 hr postendotoxin, respectively. Although the Vmax and Km for glucose-1-P for total glycogen phosphorylase were not affected by endotoxin administration, the Vmax for glucose-1-P for glycogen phosphorylase a was increased by 57.3 and 42.7% at 1 and 2 hr postendotoxin, respectively, with no change in the Km values. Glucose inhibited glycogen phosphorylase a activity both in control and endotoxin-injected dogs, but the I50 value was increased by 35% in endotoxin-injected (2 hr) dogs. AMP activated glycogen phosphorylase b activity both in control and endotoxin-injected dogs with no change in A0.5 values between the two groups.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Monophosphate↗