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PubMed1981

Effect of adrenalectomy on the diurnal variation in glycogen metabolism in starved-refed rats.

The role of glucocorticoid (GC) in the diurnal variation of glycogenesis, glycogenolysis and hepatic glycogen levels was studied in starved-refed rats. Intact, adrenalectomized (ADX) and ADX-GC supplemented rats were either ad libitum fed a 65% glucose diet or starved for 48 hours and refed the glucose diet. At the end of the starvation period and at 4-hour intervals thereafter, rats from all six treatment groups were killed and hepatic glycogen levels, glycogen synthase and phosphorylase activity determined. Ad libitum-fed animals displayed the usual diurnal glycogen and enzyme activity rhythms. Adrenalectomy was without effect in the ad libitum-fed rats on glycogen level and glycogen synthase activity and, at most points, on phosphorylase activity. Starvation-refeeding profoundly affected both the synthesis and degradation of glycogen and these effects could, in part, be attributed to the presence or absence of the adrenals. The phosphorylase activity and the hepatic glycogen level appeared to be cued by GC, whereas GC was without effect on glycogen synthase. Starvation-refeeding stimulated glycogen synthase activity within the first 4 hours of refeeding in the intact rats and within the first 8 hours of refeeding in the ADX-GC rats. These results suggest that the glycogen response to starvation refeeding is, in part, mediated by the adrenal hormones.

Adrenalectomy↗
PubMed1990

Further studies on the role of glycogenin in glycogen biosynthesis.

About 90% of the glycogenin in skeletal muscle extracts prepared from fed, 24-h starved or alloxan-diabetic rabbits sedimented at 140,000 x g with the glycogen/sarcovesicular fraction, from which it was released by glycogenolysis, but not by 1% SDS. Glycogenin in the glycogen/sarcovesicular fraction is therefore bound covalently to glycogen, and not associated (covalently or non-covalently) with the sarcoplasmic reticulum. The same proportion of glycogen synthase was also recovered in the glycogen/sarcovesicle fraction, was solubilised by glycogenolysis, and copurified with glycogenin to yield a heterodimer composed of a 1:1 complex between these proteins. Glycogen synthase and glycogenin are therefore present in equimolar amounts in skeletal muscle and there is an average of one glycogen synthase catalytic subunit associated with each molecule of glycogen in vivo. Glycogenin and glycogen synthase released into the muscle cytosol by degradation of glycogen did not form a complex initially, and only 50% reassociation took place after storage for several hours or overnight dialysis. This suggests that the muscle cytosol may contain a factor(s) which regulates glycogen biogenesis by modulating the association of glycogenin and glycogen synthase. Only glycogen synthase that was complexed to glycogenin was capable of elongating the primer formed by incubation of glycogenin with Mn2+ and micromolar concentrations of UDP-glucose, demonstrating the critical importance of this complex for glycogen biogenesis.

Animals↗
PubMed1998

Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10.

In Saccharomyces cerevisiae, PHO85 encodes a cyclin-dependent protein kinase (Cdk) with multiple roles in cell cycle and metabolic controls. In association with the cyclin Pho80, Pho85 controls acid phosphatase gene expression through phosphorylation of the transcription factor Pho4. Pho85 has also been implicated as a kinase that phosphorylates and negatively regulates glycogen synthase (Gsy2), and deletion of PHO85 causes glycogen overaccumulation. We report that the Pcl8/Pcl10 subgroup of cyclins directs Pho85 to phosphorylate glycogen synthase both in vivo and in vitro. Disruption of PCL8 and PCL10 caused hyperaccumulation of glycogen, activation of glycogen synthase, and a reduction in glycogen synthase kinase activity in vivo. However, unlike pho85 mutants, pcl8 pcl10 cells had normal morphologies, grew on glycerol, and showed proper regulation of acid phosphatase gene expression. In vitro, Pho80-Pho85 complexes effectively phosphorylated Pho4 but had much lower activity toward Gsy2. In contrast, Pcl10-Pho85 complexes phosphorylated Gsy2 at Ser-654 and Thr-667, two physiologically relevant sites, but only poorly phosphorylated Pho4. Thus, both the in vitro and in vivo substrate specificity of Pho85 is determined by the cyclin partner. Mutation of PHO85 suppressed the glycogen storage deficiency of snf1 or glc7-1 mutants in which glycogen synthase is locked in an inactive state. Deletion of PCL8 and PCL10 corrected the deficit in glycogen synthase activity in both the snf1 and glc7-1 mutants, but glycogen synthesis was restored only in the glc7-1 mutant strain. This genetic result suggests an additional role for Pho85 in the negative regulation of glycogen accumulation that is independent of Pcl8 and Pcl10.

Cyclin-Dependent Kinases↗
PubMed1979

Glycogen synthase activation in human skeletal muscle: effects of diet and exercise.

We investigated the role of glycogen synthase in supranormal resynthesis (supercompensation) of skeletal muscle glycogen after exhaustive exercise. Six healthy men exercised 60 min by cycling with one leg at 75% VO2max, recovered 3 days on a low-carbohydrate diet, exercised again, and recovered 4 days on high-carbohydrate diet. Glycogen and glycogen synthase activities at several glucose-6-phosphate (G6P) concentrations were measured in biopsy samples of m. vastus lateralis. Dietary alterations alone did not affect glycogen, whereas exercise depleted glycogen stores. After the second exercise bout, glycogen returned to normal within 24 h and reached supercompensated levels by 48 h of recovery. Glycogen synthase activation state strikingly increased after exercise in exercised muscle and remained somewhat elevated for the first 48 h of recovery in both muscles. We suggest that 1) forms of glycogen synthase intermediate to I (G6P-independent) and D (G6P-dependent) forms are present in vivo, and 2) glycogen supercompensation can in part be explained by the formation of intermediate forms of glycogen synthase that exhibit relatively low activity ratios, but an increased sensitivity to activation by G6P.

Adult↗
PubMed1991

Fetal lung development in rats with a glycogen storage disorder.

A New Zealand strain of rats (NZR/Mh) is unable to mobilize liver glycogen due to a deficiency of phosphorylase b kinase. Affected homozygous rats (gsd/gsd) were used to assess the developmental relationship between lung glycogen loss and surfactant phospholipid and protein biosynthesis. Phosphorylase a and phosphorylase b kinase activities were negligible in gsd/gsd fetal lungs compared with controls from gestational day (D18) until postnatal day 1 (D + 1). At D20, tissue glycogen content was 158 +/- 5 and 181 +/- 6 mumol/g lung for control and gsd/gsd, respectively. Control rats mobilized 84% of their lung glycogen by D + 1, whereas the gsd/gsd strain retained 70-80% of D19-20 levels. This apparent fall in gsd/gsd glycogen per gram lung was due to an increase in cellular protein and size. Thus, in controls, total glycogen per lung decreased 65% from D20 to D + 1, whereas DNA doubled. In contrast, gsd/gsd lung growth resulted in a doubling of total lung glycogen, whereas the glycogen-to-DNA ratio remained constant. A lack of cellular glycogenolysis was confirmed by electron microscopy where gsd/gsd type II cells remained large and glycogen-rich over the entire perinatal interval. The potential for glycogen breakdown by a lysosomal alpha-amyloglucosidase in gsd/gsd lungs was estimated in tissue homogenates, whereas rates of hydrolysis of glycogen or p-nitrophenylglucoside were significant and equal to controls at all ages tested. Incorporation of [14C]choline into phosphatidylcholine (PC) of incubated lung slices increased 1.7-fold in control lungs from D20-D21. Over the same interval, PC synthesis in gsd/gsd lungs was 40% lower and did not change.(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗
PubMed1978

Regulation of glycogen resynthesis in muscles of rats following exercise.

Following a strenuous bout of exercise, glycogen repletion occurred most rapidly in the fast-twitch red type of muscle, least rapidly in fast-twitch white, and at an intermediate rate in slow-twitch red muscle. There was a linear correlation between glycogen synthase I activity and the rate of glycogen synthesis in the three types of muscle. This finding helps explain the differences between the rates of glycogen resynthesis in the three muscle types, and supports the view that glycogen synthase activity is the most important factor determining the rate of glycogen synthesis when substrate supply is adequate. There was an inverse correlation between muscle glycogen concentration and percent glycogen synthase I. Plasma insulin concentration was low and norepinephrine and glucagon concentrations were elevated in the postexercise period. The finding that rapid glycogen synthesis occurred despite a hormonal milieu conducive to glycogenolysis provides evidence that a low glycogen concentration is a potent stimulus to glycogen synthesis that overrides the effects of low insulin, and high norepinephrine and glucagon levels.

Animals↗
PubMed1980

Preferential resynthesis of muscle glycogen in fasting rats after exhausting exercise.

Despite carbohydrate starvation (fasting or fat feeding) considerable glycogen accumulation, ranging from 20 to 30 mumol glucose/g, occurred in hindlimb muscles of rats following exhausting exercise that caused severe muscle and liver glycogen depletion and hypoglycemia. The largest increase in muscle glycogen occurred during the first 3 h after exercise when plasma levels of glucagon and epinephrine were very high and insulin concentration was low. The concentrations of glycogen attained in different hindlimb muscles in the fasting and fat-fed animals were between 50 and 100% of the values found in rats fed carbohydrate after the exhausting exercise. In rats fed carbohydrate following exercise, liver glycogen accumulation greatly exceeds muscle glycogen accumulation. A remarkable difference in the response of liver glycogen was seen in the carbohydrate starved rats. In contrast to the rapid increase in muscle glycogen, liver glycogen was still essentially completely depleted in the fasting and fat-fed rats 24 h after exercise. This indicates that the glucose made available via gluconeogenesis was preferentialy channeled away from liver glycogen synthesis into muscle glycogen.

Animals↗
PubMed1987

Postexercise muscle and liver glycogen metabolism in male and female rats.

Male and female Wistar rats were run for 5 min at 1.7 mph at a 17% grade to determine whether a sex difference exists in the rate of glycogen resynthesis during recovery in fast-twitch red muscle, fast-twitch white muscle, and liver. Rats were killed at one of three time points: immediately after the exercise bout, and at 1 or 4 h later. Males had significantly higher resting muscle glycogen levels (P less than 0.05). Exercise resulted in significant glycogen depletion in both sexes (P less than 0.01). Males utilized approximately 50% more glycogen during the exercise bout than females (P less than 0.05). During the food-restricted 4-h recovery period, muscle glycogen was repleted significantly during the 1st h (P less than 0.05). Liver glycogen was not depleted as a result of the exercise bout, but fell during the first h of recovery (P less than 0.05) and remained low during the subsequent 3 h. The greater glycogen utilization in red and white fast-twitch muscle during exercise by males could represent a true sex difference but could also be attributable in part to the males having performed more work as a result of 20% greater body mass. We conclude that no sex difference was observed in the rates of muscle glycogen repletion after exercise or in liver glycogen metabolism during and after exercise, and rapid postexercise muscle glycogen repletion occurred at a time of accelerated liver glycogen depletion.

Animals↗
PubMed1996

Skeletal muscle GLUT-4 and postexercise muscle glycogen storage in humans.

The purpose of this study was to examine the relationship between skeletal muscle GLUT-4 protein and postexercise glycogen storage in human subjects fed adequate carbohydrate. Eleven men completed 2 h of cycling, and a biopsy of the vastus lateralis was performed immediately after exercise cessation for the determination of muscle GLUT-4 protein and glycogen concentrations, glycogen synthase activity, and citrate synthase activity. The subjects ingested meals providing 2.0 g carbohydrate/kg body weight at 0, 2, and 4 h postexercise, and a second biopsy was performed 6 h postexercise. Muscle glycogen concentration increased significantly during the 6-h recovery period (glycogen immediately postexercise, 27.2 +/- 5.4 mmol/kg wet weight; glycogen storage, 52.4 +/- 2.9 mmol x kg wet weight-1 x 6 h-1; P<0.05). Glycogen storage during recovery was directly related to GLUT-4 protein (2.20 +/- 0.33 arbitrary standard units; r = 0.63; P<0.05) and inversely related to glycogen immediately postexercise (r = -0.70; P < 0.05). A direct correlation existed between glycogen storage during recovery and the activity of the I form of glycogen synthase (r = 0.60; P < 0.05). These results suggest that muscle GLUT-4 protein concentration, as well as factors relating to glucose disposal, may affect postexercise glycogen storage in humans fed adequate carbohydrate.

Adult↗
PubMed1990

Simultaneous synthesis and degradation of rat liver glycogen. An in vivo nuclear magnetic resonance spectroscopic study.

Using 13C nuclear magnetic resonance spectroscopic methods we examined in vivo the synthesis of liver glycogen during the infusion of D-[1-13C]glucose and the turnover of labeled glycogen during subsequent infusion of D-[1-13C]glucose. In fasted rats the processes of glycogen synthesis and degradation were observed to occur simultaneously with the rate of synthesis much greater than degradation leading to net glycogen synthesis. In fed rats, incorporation of infused D-[1-13C]glucose occurred briskly; however, over 2 h there was no net glycogen accumulated. Degradation of labeled glycogen was greater in the fed versus the fasted rats (P less than 0.001), and the lack of net glycogen synthesis in fed rats was due to degradation and synthesis occurring at similar rates throughout the infusion period. There was no indication that suppression of phosphorylase a or subsequent activation of glycogen synthase was involved in modulation of the flux of tracer into liver glycogen. We conclude that in both fed and fasted rats, glycogen synthase and phosphorylase are active simultaneously and the levels of liver glycogen reached during refeeding are determined by the balance between ongoing synthetic and degradative processes.

Animals↗
PubMed1983

Influence of circadian rhythms on rat muscle glycogen metabolism during and after exercise.

Marked circadian fluctuations in skeletal muscle glycogen concentrations have previously been reported. The purpose of the present study was to estimate the influence of these rhythms on muscle glycogen metabolism during and after high-intensity treadmill exercise. Male Sprague-Dawley rats ran five 1-min sprints at 75 m min-1 interspersed by 1-3 min rest intervals either at 08.00 h (morning) or at 20.00 h (night). All muscles sampled lost significant amounts of glycogen during exercise at both time periods. There were no differences in rates of loss between morning and night, even though glycogen levels in several muscles (high-oxidative muscles) were significantly higher before exercise in the morning. Following exercise, glycogen restoration in muscle samples primarily composed of fast-twitch fibres was more rapid in the morning than at night. There was no difference in glycogen restoration rates between the two time periods in the muscle primarily composed of slow-twitch fibres. Although liver glycogen was lower after exercise at night than in the morning, there were no differences in post-exercise blood glucose levels between the two time periods. In conclusion, circadian rhythms do not appear to influence rates of glycogen loss during high-speed running. However, since glycogen loss is the same at all times of day, one would predict that circadian changes in pre-exercise muscle glycogen concentrations would affect muscular endurance. Muscle glycogen restoration after exercise does appear to be affected by circadian rhythms, although interpretation of these data is complicated by possible changes in patterns of muscle fibre contraction at different times of the day. These circadian influences should be considered in the design of exercise studies using laboratory rodents.

Animals↗
PubMed1989

[Enzyme activity of cardiac glycogen metabolism: study of an in situ hypoxia protocol in the rat].

Myocardial hypoxia, induced by arrest of the artificial ventilation of anaesthetized open-chest rats, was utilized in order to study some aspects of the regulation of myocardial glycogen metabolism. Atenolol, a cardioselective beta-adrenergic receptor antagonist, and verapamil, an inhibitor of sarcolemmal calcium transfer, were used to determine the respective role of adenosine 3', 5'-cyclic monophosphate (cAMP) and calcium in the activation of the enzymes of glycogen phosphorolysis and synthesis. Glycogen degradation is reduced by atenolol treatment, as a consequence of a reduced activation of glycogen phosphorylase. Verapamil treatment has no significant effect, neither on the enzyme activation nor on the glycogen utilization. The activation of glycogen synthase, expressed by the conversion of the enzyme from the D to the I form, which results from the decrease in glycogen stores during hypoxia, is lowered under the effect of both drugs. However, in the beta-blocker treatment case, this effect results from a lower glycogen depletion while this effect is more specific in hearts from rats treated with verapamil. Under the effect of verapamil, the reduction of synthase activation, for a similar depletion of glycogen stores, was confirmed by experiments using isolated rat hearts submitted to ischaemia. These results show that: 1. the glycogenolysis in the hypoxic myocardium in situ is mainly controlled by a cAMP-dependent enzyme conversion or by metabolic allosteric effectors; 2. the activation of myocardial glycogen synthase, which is essentially correlated to the reduction of glycogen stores, is also calcium-dependent and most probably totally cAMP-independent.

Animals↗
PubMed1978

[Enzymes of glycogen metabolism in chick embryo liver].

At all stages of ontogenesis glycogen phosphorylase (EC 2.4.1.1) from liver chick embryos in represented by an isoenzyme whose properties are close to those of isoenzyme IL or F. Total enzyme activity (a+b forms) from the 8th day of development up to hatching gradually increases 1.5-fold, a practically complete activation of enzyme being observed by the end of embryogenesis. Phosphorylase b possesses high catalytic activity in the presence of 1 mM AMP and it activated by protamine and 0.2 M Na2SO4. Glycogen synthetase (EC 2.4.1.11) has a constant Km(UDFG) value during ontogenesis. This value is about 5.10(-4) M in the presence of 10 mM glucose-6-phosphate, both for I- and D-forms of enzyme. The total enzyme activity reaches its maximum on the 17th postembryonic day and is decreased more than 6-fold thereafter. In the course of embryogenesis the I/D ratio is increased from 0.2 on the 8th day of development up to 0,45 during extensive accumulation of glycogen and falls down to 0.33 before hatching. Glycogen biosynthesis in embryonic liver is wellcorrelated with the increase in the I/D ratio, i.e. the increase of the active form of enzyme. The proportion of granular glycogen in embryonic liver is increased from 15% up to 90% of total glycogen content between the 8th and 14th days of development. The activity of glycogen synthetase contained in granular glycogen is increased from 40% in the 8-day-old embryos up to 90% in the 18-day-old ones. The activity of phosphorylase is found in granular glycogen only on the 12th day of embryogenesis and reaches its maximum (80% of total enzyme activity) only on the 19th days of development. It is concluded that in the adult chicken liver the embronic enzymes--glycogen phosphorylase and glycogen synthetase--are retained.

Animals↗
PubMed1992

Hepatic glycogen depletion in fed female rats induced by piroxicam.

The effects of i.p. piroxicam administration on hepatic glycogen levels and enzymatic activities of key enzymes involved into glycogen metabolism in fed female rats were studied. Liver glycogen concentrations in treated rats decreased with increasing time of treatment and doses of piroxicam administered. The fall in glycogen caused by piroxicam persisted for several days after it was discontinued. Neither nadolol nor phenobarbital administration were able to prevent the depleting effect of piroxicam. In the treated rats, glucose-6-phosphatase, glycogen phosphorylase and glycogen synthase activities remained unchanged respect to control. Also, proportion of phosphorylase in the active (a) form was not significantly affected by successive piroxicam daily doses. In contrast, we demonstrated a decrease in the glycogen synthase in the active I form. This reduction was time-dependent on piroxicam treatment. Further, glucose loads were not capable to restore activity in the synthase enzyme and liver glycogen synthesis in animals treated with piroxicam. The impairment into glycogen metabolism produced by piroxicam administration suggests liver becomes unable to maintain glucose homeostasis. Furthermore, glycogen depletion might produce an impairment in the metabolism of drugs administered simultaneously with piroxicam, because biotransformation of xenobiotics is a process depending on glycogen storage in the liver cells.

Animals↗
PubMed1988

13C NMR studies of glycogen turnover in the perfused rat liver.

To assess whether hepatic glycogen is actively turning over under conditions which promote net glycogen synthesis we perfused livers from 24-h fasted rats with 20 mM D-[1-13C]glucose, 10 mM L-[3-13C]alanine, 10 mM L-[3-13C]lactate, and 1 microM insulin for 90 min followed by a 75-min "chase" period with perfusate of the same composition containing either 13C-enriched or unlabeled substrates. The peak height of the C-1 resonance of the glucosyl subunits in glycogen was monitored, in real time, using 13C NMR techniques. During the initial 90 min the peak height of the C-1 resonance of glycogen increased at almost a constant rate reflecting a near linear increase in net glycogen synthesis, which persisted for a further 75 min if 13C-enriched substrates were present during the "chase" period. However, when the perfusate was switched to the unenriched substrates, the peak height of the C-1 resonance of glycogen declined in a nearly linear manner reflecting active glycogenolysis during a time of net glycogen synthesis. By comparing the slopes of the curve describing the time course of the net [1-13C] glucose incorporation into glycogen with the rate of net loss of 13C label from the C-1 resonance of glycogen during the "chase" period we estimated the relative rate of glycogen breakdown to be 60% of the net glycogen synthetic rate. Whether this same phenomenon occurs to such an appreciable extent in vivo remains to be determined.

Alanine↗
PubMed1983

Specific mixed disulfide formation with purified bovine cardiac glycogen synthase I and glutathione.

Bovine cardiac glycogen-free glycogen synthase I reacts with oxidized glutathione at low temperature to partially inactivate the enzyme. Evidence is presented that a mixed disulfide between glutathione and the enzyme is formed in this reaction. A short incubation of the GSSG-treated enzyme with dithiothreitol restores full enzyme activity. The reaction with GSSG is pH dependent and the product is quite stable at neutral pH. Oxidation of one sulfhydryl group in glycogen synthase is associated with a loss of 60-70% of the enzyme activity. Further modification of protein sulfhydryls has less effect on the enzyme activity. Other low molecular weight disulfides also inactivate glycogen synthase and treatment with [35S]cystine to produce a 40% loss of enzyme activity gave rise to a single major radioactive peptide after cyanogen bromide digestion. Thus the GSSG-mediated inactivation of glycogen synthase apparently occurs through a single reactive sulfhydryl group that forms a mixed disulfide with low molecular weight disulfide molecules. Uridine 5'-diphosphate glucose and glycogen prevent the inactivation of glycogen-free glycogen synthase with GSSG, and glucose 6-phosphate retards the rate of inactivation. Reduction and reactivation of the GSSG-oxidized glycogen synthase is not affected by glycogen and it occurs readily at neutral pH with dithiothreitol, mercaptoethanol, or cysteamine. Oxidation of the reactive sulfhydryl group with GSSG has no effect on the rate of glycogen synthase phosphorylation by the catalytic subunit of cAMP-dependent protein kinase.

Binding Sites↗
PubMed1982

Protection of ischemic myocardium: the roles of nutrition and myocardial glycogen.

The ischemic myocardium utilizes glycogen as metabolic substrate. The effects of oral nutrition on the levels of glycogen in the myocardium and of myocardial glycogen content on myocardial tolerance to ischemia were studied. Rats were divided into groups and fed (a) rat chow, (b) rat chow plus 5% dextrose, and elemental diets (c) Flexical (Mead Johnson) or (d) Vital (Ross Laboratories). Another group was starved. All fed groups gained weight normally while the starved rats lost 23% of their body weight. Compared with the effect on rat chow, myocardial glycogen levels were elevated in the Flexical and starvation groups, while Vital depressed the level (P less than 0.01). Thus, both caloric intake and diet affected myocardial glycogen content. Elevation of myocardial glycogen content after starvation contrasted with glycogen disappearance from the liver. The level of myocardial glycogen and left ventricular function after global ischemia were correlated in dogs under cardiopulmonary bypass conditions. During 30 minutes of normothermic aortic cross-clamping, hearts with a preischemic myocardial glycogen content greater than 0.4 g% had less asystole or ventricular fibrillation. Their left ventricular function (stroke work index, myocardial contractility) upon reperfusion was substantially better than those with a myocardial glycogen level of less than 0.4 g%. Dietary manipulation and the nutritional status can thus affect the myocardial glycogen content and may be useful in protecting the myocardium from ischemia.

Animals↗
PubMed1980

Scanning microdensitometry of glycogen zonation in the livers of rats adapted to a controlled feeding schedule and to 30, 60, or 90% casein diets.

The effect of diet composition on diurnal changes in glycogen zonation patterns in rat liver was investigated in individually-caged male Sprague-Dawley rats adapted to the 2 + 22 controlled feeding and lighting schedule and to diets containing 30% casein/55% carbohydrates, 60% casein/25% carbohydrates, or 9.0% casein (30 rats/dietary group). Three rats from each dietary group were killed at the following times relative to the onset of feeding (0 min):--60, --30, 0, 15, 30, 45, 60, 90, 120, and 180 min. Glycogen in cryostat sections from the median and right lateral lobes of the liver was fixed and stained by standard techniques. The optical density of glycogen at points along the path between the central and portal veins of a given lobule was determined, and lobular glycogen gradients of replicate animals were integrated to form a composite lobular glycogen distribution profile. In the period from--60 to 0 min, liver glycogen levels were similar for rats on any of the diets, and the glycogen concentration was similar in periportal (P), midlobular (M), and centrilobular (C) hepatocytes. During the 0- to 45-min period, diet-related glycogen depletion occurred (90 > 60 > 30% casein) by asymmetrical glycogen loss (P > M > C hepatocytes) from the liver lobules. Similar food intake curves occurred for all diets. During the 45- to 180-min period, asymmetrical glycogen accumulation began in lobular parenchymal cells (P > M > C hepatocytes), and rate of accumulation was related to dietary to dietary composition (30 > 60 > 90% casein). The differential responses of parenchymal cells within liver lobules to physiological stimuli resulted in glycogen distribution changes that were rapid and of large magnitude. Our results are consistent with the hypothesis that periportal and midlobular hepatocytes are more metabolically responsive and active than centrilobular hepatocytes

Animals↗