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PubMed2000

No limiting role for glycogenin in determining maximal attainable glycogen levels in rat skeletal muscle.

We examined whether the protein level and/or activity of glycogenin, the protein core upon which glycogen is synthesized, is limiting for maximal attainable glycogen levels in rat skeletal muscle. Glycogenin activity was 27.5 +/- 1.4, 34.7 +/- 1.7, and 39.7 +/- 1.3 mU/mg protein in white gastrocnemius, red gastrocnemius, and soleus muscles, respectively. A similar fiber type dependency of glycogenin protein levels was seen. Neither glycogenin protein level nor the activity of glycogenin correlated with previously determined maximal attainable glycogen levels, which were 69.3 +/- 5.8, 137.4 +/- 10.1, and 80.0 +/- 5.4 micromol/g wet wt in white gastrocnemius, red gastrocnemius, and soleus muscles, respectively. In additional experiments, rats were exercise trained by swimming, which resulted in a significant increase in the maximal attainable glycogen levels in soleus muscles ( approximately 25%). This increase in maximal glycogen levels was not accompanied by an increase in glycogenin protein level or activity. Furthermore, even in the presence of very high glycogen levels ( approximately 170 micromol/g wet wt), approximately 30% of the total glycogen pool continued to be present as unsaturated glycogen molecules (proglycogen). Therefore, it is concluded that glycogenin plays no limiting role for maximal attainable glycogen levels in rat skeletal muscle.

Animals↗

PubMed1998

Assessment of glycogen turnover in aerobic, ischemic, and reperfused working rat hearts.

Glycogen and its turnover are important components of myocardial glucose metabolism that significantly impact on postischemic recovery. We developed a method to measure glycogen turnover (rates of glycogen synthesis and degradation) in isolated working rat hearts using [3H]- and [14C]glucose. In aerobic hearts perfused with 11 mM glucose, 1.2 mM palmitate, and 100 microU/ml insulin, rates of glycogen synthesis and degradation were 1.24 +/- 0.3 and 0.53 +/- 0. 25 micromol. min-1. g dry wt-1, respectively. Low-flow ischemia (0.5 ml/min, 60 min) elicited a marked glycogenolysis; rates of glycogen synthesis and degradation were 0.54 +/- 0.16 and 2.12 +/- 0.14 micromol. min-1. g dry wt-1, respectively. During reperfusion (30 min), mechanical function recovered to 20% of preischemic values. Rates of synthesis and degradation were 1.66 +/- 0.16 and 1.55 +/- 0. 21 micromol. min-1. g dry wt-1, respectively, and glycogen content remained unchanged (25 +/- 3 micromol/g dry wt). The assessment of glycogen metabolism needs to take into account the simultaneous synthesis and degradation of glycogen. With this approach, a substantial turnover of glycogen was detectable not only during aerobic conditions but also during ischemia as well as reperfusion.

Animals↗

PubMed1997

Fat accretion and the regulation of insulin-mediated glycogen synthesis after puberty in rats.

Peripheral insulin sensitivity decreases after puberty in both humans and rodents and can be explained mostly by a reduction in insulin-mediated glycogen synthesis. We tested the hypothesis that the increase in postpubertal fat mass (FM), reflecting an alternative energy store, regulates a decrease in the capacity to store muscle glycogen. We studied Sprague-Dawley rats (n = 21) before puberty (Pre) or after puberty (at 4 mo of age) in groups that were either ad libitum fed (Post) or moderately caloric restricted (CR). FM (by 3H2O isotope dilution technique) was decreased by >40% in CR compared with Post. Glucose uptake (Rd, by 18 mU x kg(-1) x min(-1) hyperinsulinemic clamp) was 63 +/- 8 mg x kg(-1) x min(-1) in Pre and decreased to 39 +/- 2 mg x kg(-1) x min(-1) in Post (P < 0.001). However, it increased in CR to 53 +/- 2 mg x kg(-1) x min(-1) (P < 0.001 vs. Post). This increase in Rd was mainly accounted for by an increase in glycogen synthesis (Rd glycolysis determined by the rate of conversion of 3H-labeled glucose to 3H2O) from 23 +/- 2 in Post to 33 +/- 2 mg x kg(-1) x min(-1) in CR (P < 0.001; 38 +/- 7 mg x kg(-1) x min(-1) in Pre). Correction of glycogen synthesis in CR to near-prepubertal levels was further supported by directly assayed muscle glycogen content after insulin stimulation that was 45% higher and by a 35% enhanced accumulation of [3H]glucose into glycogen. No changes in the enzyme kinetics of glycogen synthase or phosphorylase were observed. An additional group of 2-mo-old postpubertal ad libitum-fed rats was matched with CR for lean body mass but had more FM. This group demonstrated 25% lower rates of insulin-mediated glycogen synthesis compared with CR, further supporting the notion that a moderate reduction of FM prevents the decline in insulin responsiveness and glycogen synthesis occurring after puberty. These data suggest a cause-effect relationship between the increased deposition of fat and the reduced ability to store glucose in skeletal muscle after puberty.

Adipose Tissue↗

PubMed1981

Patterns of glycogen loss in muscle fibers: response to arterial occlusion during exercise.

This experiment was designed to determine if glycogen loss in active rat skeletal muscle fibers could be accentuated by periodic occlusion of blood to the muscles without significantly altering the numbers of types of fibers that lose glycogen. We attempted to augment glycogen loss by periodically occluding blood flow to the muscles while the animals ran on a treadmill. An occluder cuff was placed on the right common iliac artery of 10 rats. While the rats ran for 5 min at 26 m . min-1, blood flow to the right hindlimb was completely occluded for 16 +/- 5 (SD) s during every 30 s of the run. Glycogen loss in soleus (S), plantaris (P), and gastrocnemius (G) muscles was determined biochemically and histochemically. Muscles from both the occluded limb (S, P, and the deep red portion of G) and the nonoccluded limb (S and red G) of the runners showed significant glycogen loss compared with the controls. Furthermore, glycogen concentration was significantly lower in S, P, and red G of the occluded limb than in the same muscles of the nonoccluded limb. Significantly greater numbers of fibers within fiber type populations of P and G showed glycogen loss in the occluded limb, indicating that more motor units were recruited during the exercise bout in these muscles. The data suggest a sensitive link between motor unit recruitment and the metabolic condition of the contracting fibers, as the increased number of fibers showing glycogen loss presumably, resulted from fatigue of active units. We conclude that occlusion of blood flow to active muscles is not a feasible means of accentuating glycogen loss in active fibers while maintaining normal patterns of recruitment.

Animals↗

PubMed1987

Fiber type specific glycogen utilization in rat diaphragm during treadmill exercise.

To examine the significance of endogenous stores of glycogen in specific fiber types (I, IIa, IIb) of the costal region of the diaphragm, adult male Wistar rats performed continuous running (25 m/min, 8 degrees grade) exercise for either 30 min or until fatigue. At 30 min of exercise, glycogen loss, as measured microphotometrically using the periodic acid-Schiff technique averaged between 73 and 80% (P less than 0.05) in the different fiber types. When exercise was performed to exhaustion, representing an additional 94 min, no further reduction in glycogen was observed in any fiber type. Biochemical determinations of glycogen from the diaphragm confirmed the extensive reduction in glycogen concentration with exercise. Large reductions (P less than 0.05) in glycogen were also noted in the soleus, plantaris, and vastus lateralis red. Although significant depletion (P less than 0.05) occurred in the vastus lateralis white, it was not as pronounced as in these other muscles. Repletion to preexercise glycogen concentration was complete by 4 h of recovery in all muscles except the vastus lateralis white. It is concluded that endogenous glycogen is a significant substrate in all muscles sampled regardless of fiber composition. In the case of the costal region of the diaphragm, the increased work of breathing resulting from heavy exercise leads to the recruitment of all fiber types, and each fiber type depends on glycogen as a substrate at least early in the exercise.

Animals↗

PubMed1991

13C-NMR measurements of muscle glycogen during low-intensity exercise.

Glycogen metabolism in exercising gastrocnemius muscles was examined by natural abundance 13C nuclear magnetic resonance (NMR) spectroscopy. Five-minute 13C-NMR measurement of muscle glycogen had a reproducibility of +/- 6.5% (+/- 4.8 mM). Experiments were performed on healthy fed male and female subjects. Two protocols were followed. 1) Subjects performed plantar flexion from rest at 15, 20, or 25% of maximum voluntary contraction for up to 9 h. 2) Subjects predepleted gastrocnemius glycogen with heavy exercise and then either performed low-intensity exercise as before or rested. Gastrocnemius glycogen was measured by NMR at rest and after each hour of exercise. In some sessions, both the exercised leg and the nonexercised leg were monitored with 13C-NMR. In protocol 1, blood velocity in the femoral artery was similarly assessed with ultrasonography. During low-intensity exercise from rest (protocol 1) muscle glycogen fell to a new steady-state value after several hours and then remained constant despite continued exercise. Mean blood velocity increased ninefold within 2 min of onset of exercise and remained constant thereafter. After predepletion (protocol 2), muscle glycogen was repleted both during low-intensity exercise and at rest. After 1 h the amount of glycogen repletion was greater when coupled with light exercise [48.5 +/- 2.8 mM after 1 h of exercise, 39.7 +/- 1.1 mM after 1 h of rest (P less than 0.05)]. During subsequent light exercise, glycogen reached a steady-state value similar to that obtained in protocol 1, while in resting, recovery glycogen levels continued to increase (+2.7 mM/h) over a 7-h period.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1993

Effects of eccentric and concentric exercise on muscle glycogen replenishment.

Eccentric contractions appear to reduce muscle glycogen replenishment during the 1- to 10-day period after exercise. The main purpose of this study was to determine whether consuming a large amount of carbohydrate (1.6 g.kg-1.h-1) during the 4 h after glycogen-reducing exercise would produce different patterns of glycogen replenishment in human muscle that had undergone either eccentric or concentric contractions approximately 2 or 48 h earlier. Subjects cycled for 75 min and undertook interval exercise to deplete glycogen on days 1 and 3. After cycling exercise on day 1 only, subjects performed 10 sets of 10 repetitions of either concentric or eccentric contractions in opposite legs. During the 4 h after exercise, subjects consumed 0.4 g carbohydrate/kg body wt every 15 min. Biopsies were obtained immediately before the feedings and 4 h later, and blood was sampled every 15 min. For days 1 and 3 combined, total integrated areas for the glucose and insulin response curves averaged 1,683 mumol.ml-1.240 min-1 and 21,450 microU.ml-1.240 min-1, respectively. For days 1 and 3 combined, muscle glycogen replenishment after concentric exercise averaged 10 mmol.kg-1.h-1. On day 1 glycogen replenishment was similar for subjects performing either concentric or eccentric contractions. On day 3, however, glycogen replenishment was 25% lower (P < 0.05) in muscle that had undertaken eccentric contractions 48 h earlier than in concentrically exercised muscle. In conclusion, glycogen replenishment can be stimulated to a high rate when a large amount of carbohydrate is consumed after glycogen-depleting concentric exercise.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1997

Glycogen metabolism in the aerobic hypertrophied rat heart.

BACKGROUND: Rates of glycolysis from exogenous glucose are accelerated in hypertrophied hearts. In this study, we determined whether alterations in the metabolism of glycogen, an endogenous storage form of glucose, also occur in hypertrophied hearts. METHODS AND RESULTS: Rates of glycolysis ([3H]H2O production) and oxidation ([14C]CO2 production) from exogenous glucose and glycogen were measured in isolated working hearts from control and aortic-banded rats. Hearts in which glycogen was prelabeled with [5-(3)H]- or [U-(14)C]glucose were perfused with buffer containing 11 mmol/L [5-(3)H]- or [U-(14)C]glucose (different from the isotope used to prelabel glycogen), 0.4 mmol/L palmitate, 0.5 mmol/L lactate, and 100 microU/mL insulin. Rates of glycolysis from exogenous glucose were greater (3471+/-114 versus 2665+/-194 nmol glucose x min(-1) x g dry wt(-1), P<.05, n=4 to 6, mean+/-SEM) and rates of exogenous glucose oxidation (445+/-36 versus 619+/-16 nmol glucose x min(-1) x g dry wt(-1), P<.05, n=4 to 6) were lower in hypertrophied hearts than in control hearts. Rates of glycolysis and oxidation from glycogen were not different between hypertrophied and control hearts. A greater proportion of glycogen was oxidized (80% to 100%) than the proportion of exogenous glucose oxidized (13% to 24%) in both groups. Additionally, 10.5+/-1.4 and 12.3+/-1.0 micromol/g dry wt of glycogen was synthesized in hypertrophied and control hearts, respectively, indicating that simultaneous synthesis and degradation (ie, glycogen turnover) occurred in both groups. CONCLUSIONS: Thus, aerobic myocardial glycogen metabolism in the hypertrophied heart is similar to that observed in the normal heart even though exogenous glucose metabolism is altered in the hypertrophied heart.

Animals↗

PubMed1997

Hepatic gluconeogenic fluxes and glycogen turnover during fasting in humans. A stable isotope study.

Fluxes through intrahepatic glucose-producing metabolic pathways were measured in normal humans during overnight or prolonged (60 h) fasting. The glucuronate probe was used to measure the turnover and sources of hepatic UDP-glucose; mass isotopomer distribution analysis from [2-13C1]glycerol for gluconeogenesis and UDP-gluconeogenesis; [U-13C6]glucose for glucose production (GP) and the direct UDP-glucose pathway; and [1-2H1]galactose for UDP-glucose flux and retention in hepatic glycogen. After overnight fasting, GP (fluxes in milligram per kilogram per minute) was 2.19+/-0.09, of which 0.79 (36%) was from gluconeogenesis, 1.40 was from glycogenolysis, 0.30 was retained in glycogen via UDP-gluconeogenesis, and 0.17 entered hepatic UDP-glucose by the direct pathway. Thus, total flux through the gluconeogenic pathway (1.09) represented 54% of extrahepatic glucose disposal (2.02) and the net hepatic glycogen depletion rate was 0.93 (46%). Prolonging [2-13C1]glycerol infusion slowly increased measured fractional gluconeogenesis. In response to prolonged fasting, GP was lower (1. 43+/-0.06) and fractional and absolute gluconeogenesis were higher (78+/-2% and 1.11+/-0.07, respectively). The small but nonzero glycogen input to plasma glucose (0.32+/-0.03) was completely balanced by retained UDP-gluconeogenesis (0.31+/-0.02). Total gluconeogenic pathway flux therefore accounted for 99+/-2% of GP, but with a glycogen cycle interposed. Prolonging isotope infusion to 10 h increased measured fractional gluconeogenesis and UDP-gluconeogenesis to 84-96%, implying replacement of glycogen by gluconeogenic-labeled glucose. Moreover, after glucagon administration, GP (1.65), recovery of [1-2H1]galactose label in plasma glucose (25%) and fractional gluconeogenesis (91%) increased, such that 78% (0.45/0.59) of glycogen released was labeled (i.e., of recent gluconeogenic origin). In conclusion, hepatic gluconeogenic flux into glycogen and glycogen turnover persist during fasting in humans, reconciling inconsistencies in the literature and interposing another locus of control in the normal pathway of GP.

Carbon Isotopes↗

PubMed1996

An antidiabetic thiazolidinedione potentiates insulin stimulation of glycogen synthase in rat adipose tissues.

Thiazolidinedione derivatives are a novel class of insulin-sensitizing agents that have demonstrated effective antidiabetic activity in vivo. Here, the effects of the potent thiazolidinedione derivative, AD-5075, on the rate-limiting enzyme of glycogen synthesis, glycogen synthase, were investigated in cultured rat adipose tissue. Short term preincubation of adipose tissue with AD-5075 potentiated acute insulin stimulation of I-form glycogen synthase activity in a concentration-dependent (EC50 approximately, 61nM) and time-dependent (t1/2 approximately, 2.3 h) manner. The thiazolidinedione derivative increased the responsiveness of I-form glycogen synthase activity to insulin stimulation at both maximal and submaximal insulin concentrations. In contrast, it had no effect on total glycogen synthase activity. Isoproterenol inhibited acute insulin activation of I-form glycogen synthase activity in a dose-dependent manner; maximal inhibition was attained at a concentration of 3 nM. AD-5075 antagonized isoproterenol inhibition of insulin's action. The concentration of glycogenolytic agent required to attain maximal inhibition was increased an order of magnitude in tissue treated with the antidiabetic agent. Short term preincubation of adipose tissue under hyperglycemic conditions (15 or 25 mM glucose) decreased insulin-stimulated I-form glycogen synthase activity. Concurrent treatment of the tissue with AD-5075 abrogated this glucose toxicity-induced inhibition of insulin action. Wortmannin, an inhibitor of phosphatidylinositol 3-kinase, blocked insulin activation of glycogen synthase in a dose-dependent manner. Half-maximal inhibition was observed at approximately 0.3 microM, and maximal inhibition occurred at 1.0 microM. AD-5075 did not antagonize wortmannin's inhibitory action. These results indicate that thiazolidinediones can act directly on adipose tissues to augment an important metabolic effect of insulin and counteract the inhibitory effects of catecholamines or hyperglycemia. As insulin stimulation of glycogen synthase remains wortmannin inhibitable in the presence of AD-5075, the effects of thiazolidinediones on insulin signal transduction may be phosphatidylinositol 3-kinase-dependent.

Adipose Tissue↗

PubMed2003

Glycogen synthesis in muscle fibers during active recovery from intense exercise.

PURPOSE: There is evidence that active recovery impairs glycogen repletion in skeletal muscles of fasted individuals. Our main goal was to examine the impact of active recovery on the glycogen stores of the different muscle fiber types. METHODS: Eight endurance-trained individuals cycled for 2.5 min at 130% [OV0312]O(2peak) followed by a 30-s all-out cycling sprint. After exercise, the participants were subjected to either a passive recovery or an active recovery protocol that consisted of pedalling for 45 min at 40% [OV0312]O(2peak). RESULTS: During active recovery, blood lactate and pH returned more rapidly toward preexercise levels than during passive recovery. In contrast, average muscle glycogen content remained at stable levels during active recovery (209 +/- 32 and 202 +/- 30 mmol.kg-1 at 0 and 45 min of recovery, respectively) but increased significantly in response to passive recovery (from 185 +/- 27 to 283 +/- 42 mmol.kg-1). The pattern of change in periodic acid-Schiff staining intensity across muscle fibers suggests that the impact of active recovery on average muscle glycogen content is different from that observed at the levels of the individual muscle fibers, with active recovery having no effect on glycogen resynthesis in Type II muscle fibers but causing glycogen breakdown in Type I muscle fibers. Although active recovery was also associated with higher plasma catecholamines and lower insulin levels, such an unfavorable hormonal environment had no effect on glycogen resynthesis in Type II muscle fibers. CONCLUSION: Active recovery in comparison to passive recovery does not affect glycogen resynthesis in Type II muscle fibers despite being associated with an unfavorable hormonal environment but results in a marked glycogen mobilization in Type I muscle fibers.

Adult↗

PubMed1996

Insulin stimulates protein synthesis of glycogen synthase in rat hepatoma H4 cells associated with acceleration of translation rate.

To assess the regulatory mechanism of insulin action on the biosynthesis of glycogen synthase under long-term control, we investigated post-transcriptional and post-translational regulation by insulin of glycogen synthase in rat hepatoma H4 cells. Glycogen synthase protein gradually increased in response to insulin and peaked at 6 h during a 24-h insulin incubation (185% of the control), corresponding with the second peak of glycogen synthase activation measured by the activity ratio (low glucose 6-P/high glucose 6-P). The effect of insulin on synthesis of glycogen synthase protein was assessed by measuring the incorporation of [35S]-methionine into the enzyme protein during a 6-h insulin incubation. The amount of [35S]-methionine incorporation into glycogen synthase was increased in response to insulin with time, and peaked at 4 h (250% of the control). The degradation of glycogen synthase examined by measuring the rate of reduction of [35S]-methionine for 6 h after the tracer incubation for 12 h was not affected by insulin. The results indicate that (a) insulin induces glycogen synthase activity by accumulating the enzyme protein due to stimulation of protein synthesis rather than inhibition of protein degradation and (b) insulin-reduced stability of glycogen synthase mRNA is caused by acceleration of the translation rate.

Amino Acid Sequence↗

PubMed1988

Hormonal regulation of glycogen synthase and phosphorylase activities in human polymorphonuclear leukocytes.

Hormonal regulation of glycogen synthase and phosphorylase activities were studied in human polymorphonuclear leukocytes. Polymorphonuclear leukocytes from normal subjects were incubated with glucose, insulin, D,L-isoproterenol and L-thyroxine, either independently or in different combinations, and changes of the enzyme activity ratios of glycogen synthase (active form (I)/total activity (T)) and glycogen phosphorylase (active form (a)/total activity (T)) were assessed. Neither glucose nor insulin changed the glycogen synthase activity ratio. However, the proportion of the active form (I) of glycogen synthase was increased by the simultaneous addition of glucose and insulin to the incubation mixture, but D,L-isoproterenol or L-thyroxine diminished this effect and caused a decrease in the proportion of the active form of glycogen synthase. Insulin had no effect on the glycogen phosphorylase activity ratio. Glucose decreased the proportion of phosphorylase in the a form. The simultaneous addition of glucose and insulin caused no further changes, whereas in the presence of D,L-isoproterenol or L-thyroxine, this glucose effect was abolished and the proportion of phosphorylase a increased. These results show that both thyroid hormone and a beta-agonist alter glycogen metabolism to reduce glycogen storage in polymorphonuclear leukocytes.

Drug Interactions↗

PubMed2002

Effect of glimepiride on insulin-stimulated glycogen synthesis in cultured human skeletal muscle cells: a comparison to glibenclamide.

OBJECTIVE: To examine the effect of glimepiride on insulin-stimulated glycogen synthesis in cultured human skeletal muscle cells in comparison with glibenclamide. RESEARCH DESIGN AND METHODS: Myotubes derived from glucose-tolerant subjects were incubated with glimepiride or glibenclamide (0-100 micro mol/l) for 4 h and with or without insulin (100 nmol/l) for 2 h, and subsequently glycogen synthesis was determined. RESULTS: Glimepiride had no significant effect on basal glycogen synthesis; in contrast, glimepiride caused a dose-dependent increase of insulin-stimulated glycogen synthesis, with a maximal effect of 39.97 +/- 8.4% (mean +/- SEM, n = 4, P < 0,02). The time course of this glimepiride effect on insulin-stimulated glycogen synthesis showed a peak after 12 h incubation with a half maximal effect after 4 h. Preincubation of the myotubes with wortmannin (100 nmol/l), an inhibitor of phosphatidylinositol (PI)- 3 kinase, caused an inhibition of this glimepiride effect on insulin-stimulated glycogen synthesis. In contrast to glimepiride, incubation of myotubes with glibenclamide (0-100nmol/l), a second generation sulfonylurea, had no significant effect on basal or insulin-stimulated glycogen synthesis. CONCLUSIONS: Incubation of cultured human skeletal muscle cells derived from glucose-tolerant subjects with glimepiride caused a dose-dependent increase of insulin-stimulated glycogen synthesis using therapeutic glimepiride concentrations. This glimepiride effect seems to be mediated via the PI3 kinase pathway. In contrast to glimepiride, glibenclamide had no significant effect on basal or insulin-stimulated glycogen synthesis. These results suggest that glimepiride, beside its well-known effect to stimulate insulin secretion, possess an insulin-sensitizing action in cultured human skeletal muscle cells in support of the concept of an extrapancreatic action of glimepiride.

Androstadienes↗

PubMed2002

Brain glycogen decreases with increased periods of wakefulness: implications for homeostatic drive to sleep.

Sleep is thought to be restorative in function, but what is restored during sleep is unclear. Here we tested the hypothesis that increased periods of wakefulness will result in decreased levels of glycogen, the principal energy store in brain, and with recovery sleep levels of glycogen will be replenished, thus representing a homeostatic component of sleep drive. Using a high-energy focused microwave irradiation method to kill animals and thereby snap-inactivate glycogen-producing and -metabolizing enzymes, we determined, with accuracy and precision, levels of brain glycogen and showed these levels to decrease significantly by approximately 40% in brains of rats deprived of sleep for 12 or 24 hr. Recovery sleep of 15 hr duration after 12 hr of sleep deprivation reversed the decreases in glycogen. Using a novel histochemical method to stain brain glycogen, we found glycogen to be concentrated in white matter; this finding was confirmed biochemically in white matter dissected from rats killed with microwave irradiation. Levels of glycogen, as determined histochemically, were significantly decreased in gray and white matter with sleep deprivation, and these decreases were reversed with recovery sleep. The observed decreases in levels of brain glycogen may be a consequence of increased wakefulness and/or a component integral to the homeostatic drive to sleep.

Animals↗

PubMed1976

Role of cortisol on the glycogenolytic effect of glucagon and on the glycogenic response to insulin in fetal hepatocyte culture.

The effects of insulin and glucagon on glycogen metabolism were studied in cultured fetal hepatocytes transplanted from 15-day-old fetuses. The effects of these hormones were examined just after transplantation, when the cells contained only minute amounts of glycogen, and during the 3 to 4 day culture period, when the hepatocytes were exposed to 10 muM cortisol and actively accumulated glycogen. At all stages of the culture, glucagon addition (10 nM) was followed by a rapid depletion of labeled glycogen, previously synthesized during a pulse labeling with [14C]glucose: this effect was mimicked by N6, O2'-dibutyryl adenosine 3':5'-monophosphate (dibutyryl cyclic AMP) (0.3 to 1 nM). Such a glycogenolytic effect of glucagon was observed even 6 hours after transplantation, i.e. at a time when cortisol was not present. In addition, glucagon clearly induced cyclic adenosine 3':5'-monosphosphate (cyclic AMP) accumulation in cells grown for 18 hours in the absence of cortisol. With cells grown for 3 days in the presence of cortisol, glucagon-dependent glycogenolysis was also obtained when cortisol was removed from the medium 20 hours before hormone addition. Thus the presence of cortisol is not necessary either to maintain a response to glucagon or for the onset of the glycogenolytic effect of glucagon. Insulin addition (10 nM) stimulated [14C]glucose incorporation into glycogen at all stages of the culture when grown in the presence of cortisol; no glycogenic response to insulin was observed 6 hours after transplantation where cortisol was not previously introduced. In addition, if the hepatocytes were grown in the presence of insulin alone (i.e. in the absence of cortisol) no significant storage of glycogen occurred. Maximal storage (or labeling) of glycogen was observed when hepatocytes were grown in the presence of both cortisol and insulin. The presence of cortisol was therefore necessary for the expression of the glycogenic effect of insulin. These data show that marked difference exist between the onset of developmental responses towards glucagon and insulin. The glucagon-dependent regulatory pathway should be present very early in fetal development and should not depend on cortisol. On the contrary, the onset of the insulin-dependent regulatory pathway seems to be induced during culture, and it is likely that this is caused by cortisol.

Animals↗

PubMed1989

[The role of phosphorylase kinase subunits in interaction with glycogen].

The interaction of rabbit skeletal muscle phosphorylase kinase with CNBr-activated glycogen results in the formation of a covalent complex. The non-bound kinase was removed by chromatography on DEAE-cellulose and phenyl-Sepharose. The amount of the bound protein increased with an increase in the number of activated groups in the glycogen molecule; the enzyme activity was thereby decreased. The kinase covalently and non-covalently bound to glycogen exhibited a higher affinity for the protein substrate (phosphorylase b) as well as for Mg2+ and Ca2+ than did the kinase in the absence of glycogen. Electrophoresis performed under denaturating conditions showed that the gamma-subunit of phosphorylase kinase is responsible for the enzyme binding to CNBr-glycogen. The effect of cross-linking reagents (glutaric aldehyde, 1.5-difluoro-2.4-dinitrobenzene) on the binding of phosphorylase kinase subunits was studied. Glycogen afforded protection of the gamma-subunit from the cross-linking to other enzyme subunits. An analysis of the subunit composition of phosphorylase kinase covalently bound to CNBr-glycogen and of the enzyme treated with cross-linking reagents in the presence of glycogen-revealed that the gamma-subunit is involved in the specific binding of phosphorylase kinase to glycogen.

Animals↗

PubMed1979

Importance of preoperative myocardial glycogen levels in human cardiac preservation. Preliminary report.

One hundred seventeen patients undergoing elective coronary bypass were divided into four groups according to prebypass myocardial glycogen levels and the use of potassium chloride cardioplegia. Myocardial glycogen levels were enhanced with a preoperative fat loading diet and overnight glucose loading. The control group (n = 27) which had mean cardiac glycogen levels of 750 mg/100 gm heart weight and no cardioplegia, had a transmural myocardial infarct rate of 14.4%; 35% had severe atrial arrhythmias 65% had severe ventricular arrhythmias, and 31% had severe vasopressor dependence. The group (n = 30) with low cardiac glycogen (736 mg/100 gm) and with potassium chloride cardioplegia had an infarct rate of 6.4%; 6.7% had severe atrial arrhythmias, 18% had severe ventricular arrhythmias, and 16.7% had severe vasopressor dependence. However, the group (n = 26) which had high cardiac glycogen levels (1,208 mg/100 gm) and no cardioplegia had no myocardial infarctions; 3.8% had severe atrial arrhythmias, 27% had severe ventricular arrhythmias, and only 7.8% had severe vasopressor need. The group (n = 34) which had high glycogen levels (1,516 mg/100 gm) and potassium chloride cardioplegia did best of all with no myocardial infarctions or no severe atrial arrhythmias; 14% had severe ventricular arrhythmias and 2.81% severe vasopressor need. The lessening of vasopressor dependence and severe atrial and ventricular arrhythmias were significant by chi square contingency tables at p less than 0.05 and p less than 0.001, respectively. One cardiac-related death each occurred in the two groups with low glycogen and none in those with high glycogen levels. This suggests that better preoperative cardiac nutrition as represented by enhanced cardiac glycogen helps that heart tolerate anoxic stress whether cardioplegia is utilized or not and is additive to potassium chloride cardioplegia.

Aorta↗