PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “GLYCOGEN”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 901 records · Page 50Linked to original sources

Regulation of glycogen metabolism in canine myocardium: effects of insulin and epinephrine in vivo.

Myocardial glycogen synthesis and glucose, lactate, and oxygen extraction were measured in the hearts of anesthetized dogs during infusions of insulin and epinephrine. Glycogen was monitored in vivo using 13C-nuclear magnetic resonance during an infusion of [1-13C]glucose into the left anterior descending artery. Glycogen synthesis was observed during a venous infusion of insulin (1.8 microU.min-1.kg-1), and this newly synthesized glycogen was neither broken down nor was more glycogen synthesized during a subsequent epinephrine infusion (0.5 micrograms.min-1.kg-1). During recovery from epinephrine, glycogen synthesis occurred at 2.1 times the rate seen in the control period. Glycogen synthesis was not stimulated in the absence of epinephrine by control infusions of saline. Glucose uptake was increased by insulin during the control period (from 0.09 to 0.39 mumol.min-1.g-1), so that the combined extraction of glucose and lactate exceeded the requirement for oxidizable substrate calculated from oxygen consumption. The "excess" glucose (0.15 mumol.min-1.g wet wt-1) is presumably available for glycogen synthesis. During recovery from epinephrine, lactate uptake was increased over threefold. Because this additional lactate supplies most of the fuel required for oxidation, the excess glucose available for glycogen synthesis during this period was two times that seen before epinephrine (an average of 0.32 mumol.min-1.g wet wt-1 between 20 and 40 min postepinephrine). These data are consistent with the notion that glycogen synthesis can be activated in the heart without an accompanying increase in glucose uptake by providing an alternative substrate (i.e., lactate) for oxidation.

Animals↗

Liver glycogen turnover in fed and fasted humans.

Whether liver glycogen synthesis and breakdown occur simultaneously during net glycogen synthesis was assessed in fed and fasted healthy humans. The peak intensity of the carbon-1 (C1) resonance of the glycosyl units of glycogen was monitored with 13C nuclear magnetic resonance spectroscopy during [1-13C]glucose infusion followed by unlabeled glucose infusion. The C1 peak intensity increased almost linearly during the [1-13C]glucose infusion, reflecting a near linear rate of glycogen synthesis. When switched to unlabeled glucose, the C1 peak intensity reached a plateau in the fasted subjects and declined in the fed subjects, reflecting active glycogenolysis during a time of net glycogen synthesis. We conclude that liver glycogen synthesis and degradation occur simultaneously in humans under conditions of net glycogen synthesis. The relative turnover rate was significantly higher in the fed (57 +/- 3%) than in the fasted state (31 +/- 8%; P < 0.01). The results indicate that glycogen may regulate its rate of breakdown and that liver glycogen turnover may be an important factor in limiting the accumulation of liver glycogen in humans.

Adult↗

Increased concentrations of glycogen synthase protein in skeletal muscle of patients with NIDDM.

To examine whether changes in the glycogen synthase protein concentration contribute to impaired insulin-stimulated glycogen metabolism in patients with noninsulin-dependent diabetes mellitus (NIDDM), muscle biopsies were taken before and after a 4-h euglycemic hyperinsulinemic clamp to measure glycogen synthase activity and glycogen synthase protein concentrations in 14 patients with NIDDM and in 17 control subjects. Nonoxidative glucose metabolism was reduced by 64% in patients with NIDDM compared with control subjects and correlated with insulin-stimulated glycogen synthase activity (r = 0.55, P < 0.05). The concentration of glycogen synthase protein in skeletal muscle was higher in patients with NIDDM than in control subjects (6.75 +/- 0.88 vs. 4.41 +/- 0.50 counts.min-1.micrograms protein-1, P < 0.05), whereas there was no significant difference in glycogen synthase mRNA concentration between the two groups. The glycogen synthase protein concentration correlated inversely with the rate of nonoxidative glucose metabolism (r = -0.63, P < 0.05). These findings indicate that the amount of glycogen synthase protein is increased in skeletal muscle of patients with NIDDM. The increase in the glycogen synthase protein may serve to compensate for a functional defect in the activation of the enzyme by insulin.

Blood Glucose↗

Energy provision from glycogen, glucose, and fatty acids on adrenergic stimulation of isolated working rat hearts.

We postulated that glycogen is a significant energy substrate compared with fatty acids and glucose in response to adrenergic stimulation of working rat hearts. Oxidation rates were determined at 1-min intervals by release of 3H2O from [9,10-(3)H]oleate (0.4 mM, 1% albumin) and 14CO2 from exogenous [U-14C]glucose (5 mM) or, by a pulse-chase method, from [14C]glycogen. We estimated the 14C enrichment of glycogen metabolized at each time point to determine true rates of glycogen use. Based on the pattern of glycogen enrichment over time, glycogenolysis did not exhibit a high degree of preference for newly synthesized glycogen. Epinephrine (1 microM) increased contractile performance 86% but did not stimulate oleate oxidation. The increased energy demand was supplied by carbohydrates, initially by a burst of glycogenolysis (contributing 35% to total ATP synthesis for 5 min) and followed by delayed increase in the use of exogenous glucose (eventually contributing 29% to ATP synthesis). On the basis of the release of 14CO2 and [14C]lactate specifically from glucose or glycogen, we found that a larger portion of glycogen was oxidized compared with exogenous glucose, augmenting the yield of ATP from glycogen. Thus the heart responds to an acute increase in energy demand by selective oxidation of glycogen.

Adenosine Triphosphate↗

Muscle glycogen recovery after exercise during glucose and fructose intake monitored by 13C-NMR.

The purpose of this study was to examine muscle glycogen recovery with glucose feeding (GF) compared with fructose feeding (FF) during the first 8 h after partial glycogen depletion using 13C-nuclear magnetic resonance (NMR) on a clinical 1.5-TNMR system. After measurement of the glycogen concentration of the vastus lateralis (VL) muscle in seven male subjects, glycogen stores of the VL were depleted by bicycle exercise. During 8 h after completion of exercise, subjects were orally given either GF or FF while the glycogen content of the VL was monitored by 13C-NMR spectroscopy every second hour. The muscular glycogen concentration was expressed as percentage of the glycogen concentration measured before exercise. The glycogen recovery rate during GF (4.2 +/- 0.2%/h) was significantly higher (P < 0.05) compared with values during FF (2.2 +/- 0.3%/h). This study shows that 1) muscle glycogen levels are perceptible by 13 C-NMR spectroscopy at 1.5 T and 2) the glycogen restoration rate is higher after GF compared with after FF.

Adult↗

Regulation of exogenous and endogenous glucose metabolism by insulin and acetoacetate in the isolated working rat heart. A three tracer study of glycolysis, glycogen metabolism, and glucose oxidation.

Myocardial glucose use is regulated by competing substrates and hormonal influences. However, the interactions of these effectors on the metabolism of exogenous glucose and glucose derived from endogenous glycogen are not completely understood. In order to determine changes in exogenous glucose uptake, glucose oxidation, and glycogen enrichment, hearts were perfused with glucose (5 mM) either alone, or glucose plus insulin (40 microU/ml), glucose plus acetoacetate (5 mM), or glucose plus insulin and acetoacetate, using a three tracer (3H, 14C, and 13C) technique. Insulin-stimulated glucose uptake and lactate production in the absence of acetoacetate, while acetoacetate inhibited the uptake of glucose and the oxidation of both exogenous glucose and endogenous carbohydrate. Depending on the metabolic conditions, the contribution of glycogen to carbohydrate metabolism varied from 20-60%. The addition of acetoacetate or insulin increased the incorporation of exogenous glucose into glycogen twofold, and the combination of the two had additive effects on the incorporation of glucose into glycogen. In contrast, the glycogen content was similar for the three groups. The increased incorporation of glucose in glycogen without a significant change in the glycogen content in hearts perfused with glucose, acetoacetate, and insulin suggests increased glycogen turnover. We conclude that insulin and acetoacetate regulate the incorporation of glucose into glycogen as well as the relative contributions of exogenous glucose and endogenous carbohydrate to myocardial energy metabolism by different mechanisms.

Acetoacetates↗

Delay in pulmonary glycogen degradation in fetuses of streptozotocin diabetic rats.

The developmental profile of pulmonary glycogen was investigated in fetuses of rats made diabetic before conception with the injection of 40 mg/kg streptozotocin. Lungs of control litters showed increasing pulmonary glycogen concentration from day 16-20, followed by significant decline by term (= 22 days). In contrast, the diabetic litters, which had pulmonary glycogen concentration equal to controls until day 20, showed significantly higher glycogen values (P less than 0.01) on days 21 and 22, consistent with a delay in glycogen degradation. This coincided with the finding of decreased amounts of fetal pulmonary phosphatidylcholine and disaturated phosphatidylcholine on day 21 of the diabetic gestation (P less than 0.05), but not before that time. Pulmonary glycogen phosphorylase A activity was significantly decreased in the diabetic litters on the final days of gestation, at the same time that the delay in glycogen breakdown became evident. Pulmonary glycogen synthase activity did not differ in the control and diabetic fetuses. The delay in pulmonary glycogen degradation seen in the fetus of the diabetic gestation is thus temporally related to the delay in lung maturation seen in this model and may be secondary to a decrease in the activity of the glycogenolytic enzyme phosphorylase A. Decreased availability of pulmonary glycogen stores for surfactant synthesis may be important in elucidating the mechanism of the delayed pulmonic maturation seen in fetuses of diabetic pregnancies.

Animals↗

Laforin targets malin to glycogen in Lafora progressive myoclonus epilepsy.

Glycogen is the largest cytosolic macromolecule and is kept in solution through a regular system of short branches allowing hydration. This structure was thought to solely require balanced glycogen synthase and branching enzyme activities. Deposition of overlong branched glycogen in the fatal epilepsy Lafora disease (LD) indicated involvement of the LD gene products laforin and the E3 ubiquitin ligase malin in regulating glycogen structure. Laforin binds glycogen, and LD-causing mutations disrupt this binding, laforin-malin interactions and malin's ligase activity, all indicating a critical role for malin. Neither malin's endogenous function nor location had previously been studied due to lack of suitable antibodies. Here, we generated a mouse in which the native malin gene is tagged with the FLAG sequence. We show that the tagged gene expresses physiologically, malin localizes to glycogen, laforin and malin indeed interact, at glycogen, and malin's presence at glycogen depends on laforin. These results, and mice, open the way to understanding unknown mechanisms of glycogen synthesis critical to LD and potentially other much more common diseases due to incompletely understood defects in glycogen metabolism.

Animals↗

Muscle triglyceride and glycogen in endurance exercise: implications for performance.

The importance of muscle glycogen as a metabolic substrate in sustaining prolonged exercise is well acknowledged. Being stored in proximity to the site of contraction and able to sustain high rates of adenosine diphosphate (ADP) phosphorylation, glycogen is viewed as the primary fuel for the maintenance of exercise of a moderate to intense nature. As such, to ensure optimal exercise performance, endurance athletes are encouraged to maximise the availability of muscle glycogen through the ingestion of a high carbohydrate (CHO) diet prior to competition. The skeletal muscle cell also contains significant quantities of triglyceride. Recent improvements in the ability to measure these intramyocellular triglyceride (IMTG) stores have confirmed that IMTG acts as a significant fuel substrate during prolonged exercise. While early research of the role of muscle glycogen in endurance exercise provided clear prescriptive information for the endurance-trained athlete, no such direction for optimising exercise performance is yet apparent from research concerning IMTG. In this article, we review the processes of muscle glycogen and triglyceride storage and metabolism. Attention is given to the effects of short-term alterations in diet on muscle substrate, particularly IMTG storage, and the implications of this to endurance exercise performance and competition preparation. We demonstrate that like glycogen, IMTG formation may be relatively rapid, and its storage predominates under conditions that promote minimal glycogen formation. This observation suggests that the role of IMTG is to maintain a readily available substrate to ensure that physical activity of a moderate nature can be performed when glycogen availability is not optimal. Under these conditions, IMTG may offer a similar availability of energy as glycogen in the endurance-trained athlete. Given the potential value of this substrate, the possibility of maximising IMTG storage without compromising glycogen availability prior to competition is considered.

Energy Metabolism↗

Structure and segmental localization of glycogen in the diabetic rat kidney.

Pathological accumulations of glycogen were studied in the kidney tubular epithelium in untreated STZ-induced diabetic rats of 50 days diabetes duration. Blood glucose concentrations were approximately 17 mM, and the animals had no ketonuria. At the termination of the experiment, the kidneys were perfusion-fixed, and serial sections were cut from the renal capsule to the tip of the papilla and stained with toluidine blue and periodic acid Schiff. By tracing tubular profiles from section to section in a light microscope, the outlines of nephrons were reconstructed, and abnormal glycogen accumulations were mapped in accordance with the outlines. The exact segmental localization, character, and extension of the glycogen accumulations were determined. The predominant location of the pathological glycogen accumulations was in the thick ascending limb of Henle's loop. Dot-shaped and diffuse-appearing glycogen accumulations were discretely distributed throughout the segment, and large confluent cytoplasmic accumulations of glycogen were also present. On a continuous basis, glycogen was present only in the cortical thick ascending limb of Henle's loop and the macula densa segment excluding the macula densa cells. In the distal convoluted tubule and the cortical collecting duct system, scattered dot-shaped and diffuse glycogen accumulations were discretely distributed. Furthermore, glycogen appeared as confluent, cytoplasmic accumulations in the initial part of the descending thin limb of Henle's loop. In addition, glycogen accumulations were found in nuclei within a narrow stripe of the outer stripe of the outer medulla in the medullary thick ascending limb of Henle's loop.

Animals↗

Effects of short-term improvement of insulin treatment and glycemia on hepatic glycogen metabolism in type 1 diabetes.

Insufficiently treated type 1 diabetic patients exhibit inappropriate postprandial hyperglycemia and reduction in liver glycogen stores. To examine the effect of acute improvement of metabolic control on hepatic glycogen metabolism, lean young type 1 diabetic (HbA1c 8.8 +/- 0.3%) and matched nondiabetic subjects (HbA1c 5.4 +/- 0.1%) were studied during the course of a day with three isocaloric mixed meals. Hepatic glycogen concentrations were determined noninvasively using in vivo 13C nuclear magnetic resonance spectroscopy. Rates of net glycogen synthesis and breakdown were calculated from linear regression of the glycogen concentration time curves from 7:30-10:30 P.M. and from 10:30 P.M. to 8:00 A.M., respectively. The mean plasma glucose concentration was approximately 2.4-fold higher in diabetic than in nondiabetic subjects (13.6 +/- 0.4 vs. 5.8 +/- 0.1 mmol/l, P < 0.001). Rates of net glycogen synthesis and net glycogen breakdown were reduced by approximately 74% (0.11 +/- 0.02 vs. 0.43 +/- 0.04 mmol/l liver/min, P < 0.001) and by approximately 47% (0.10 +/- 0.01 vs. 0.19 +/- 0.01 mmol/l liver/min, P < 0.001) in diabetic patients, respectively. During short-term (24-h) intensified insulin treatment, the mean plasma glucose level was not different between diabetic and nondiabetic subjects (6.4 +/- 0.1 mmol/l). Net glycogen synthesis and breakdown increased by approximately 92% (0.23 +/- 0.04 mmol/l liver/min, P = 0.017) and by approximately 40% (0.14 approximately 0.01 mmol/l liver/min, P = 0.011), respectively. In conclusion, poorly controlled type 1 diabetic patients present with marked reduction in both hepatic glycogen synthesis and breakdown. Both defects in glycogen metabolism are improved but not normalized by short-term restoration of insulinemia and glycemia.

Adult↗

Kinetics of the interaction of rabbit skeletal muscle phosphorylase kinase with glycogen.

The kinetics of the interaction of rabbit skeletal muscle phosphorylase kinase with glycogen was studied by the turbidimetric method at pH 6.8 and 8.2. Binding of phosphorylase kinase by glycogen occurs only in the presence of Ca2+ and Mg2+. The initial rate of complex formation is proportional to the enzyme and polysaccharide concentration; this suggests the formation of a complex with 1:1 stoichiometry in the initial step of phosphorylase kinase binding by glycogen. The kinetic data suggest that phosphorylase kinase substrate--glycogen phosphorylase b--favors the binding of phosphorylase kinase with glycogen. This conclusion is supported by direct experiments on the influence of phosphorylase b on the interaction of phosphorylase kinase with glycogen using analytical sedimentation analysis. The kinetic curves of the formation of the complex of phosphorylase kinase with glycogen obtained in the presence of ATP are characterized by a lag period. Preincubation of phosphorylase kinase with ATP in the presence of Ca2+ and Mg2+ causes the complete disappearance of the lag period. On changing the pH from 6.8 to 8.2, the rate of phosphorylase kinase binding by glycogen is appreciably increased, and complex formation becomes possible even in the absence of Mg2+. A model of phosphorylase kinase and phosphorylase b adsorption on the surface of the glycogen particle explaining the increase in the strength of phosphorylase kinase binding with glycogen in the presence of phosphorylase b is proposed.

Adenosine Triphosphate↗

Protein targeting to glycogen mRNA expression is stimulated by noradrenaline in mouse cortical astrocytes.

Brain glycogen levels are dynamically regulated by certain neurotransmitters, including noradrenaline (NA) and vasoactive intestinal peptide (VIP). In particular, glycogen synthesis involves activation by NA and VIP of the transcription factors C/EBPbeta and -delta as well as the induction of glycogen synthase. Glycogen accumulation is found in a variety of neuropathological conditions, including reactive astrocytosis after CNS lesions, as well as in Alzheimer's disease. Protein targeting to glycogen (PTG) belongs to a family of proteins that play a key role in glycogen synthesis in peripheral tissues. In this study, we report the presence of PTG mRNA in adult mouse brain, as well as in astrocytes, a non-neuronal cell type that contains most of brain glycogen. Using primary cultures of mouse cortical astrocytes, we observed that NA leads to time- and concentration-dependent induction of PTG mRNA expression. This effect, concomitant to an enhancement of glycogen synthesis in these cells, depends on the activation of beta(1)-adrenergic receptors. Induction of PTG mRNA expression was mimicked by the adenylate cyclase activator forskolin and by dibutyryl cAMP, suggesting the involvement of the cAMP-dependent signal transduction cascade. Among other neuroactive substances known to elevate glycogen levels in astrocytes, VIP had a comparable effect to that of noradrenaline, whereas insulin and glutamate were without effect on PTG mRNA expression. These data suggest that increased PTG expression by neurotransmitters such as noradrenaline and VIP could represent a major event leading to enhancement of glycogen levels in astrocytes.

Animals↗

Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by distinct genes that are differentially controlled.

In previous work, we identified a Saccharomyces cerevisiae glycogen synthase gene, GSY1, which codes for an 85-kDa polypeptide present in purified yeast glycogen synthase (Farkas, I., Hardy, T.A., DePaoli-Roach, A.A., and Roach, P.J. (1990) J. Biol. Chem. 265, 20879-20886). We have now cloned another gene, GSY2, which encodes a second S. cerevisiae glycogen synthase. The GSY2 sequence predicts a protein of 704 residues, molecular weight 79,963, with 80% identity to the protein encoded by GSY1. Amino acid sequences obtained from a second polypeptide of 77 kDa present in yeast glycogen synthase preparations matched those predicted by GSY2. GSY1 resides on chromosome VI, and GSY2 is located on chromosome XII. Disruption of the GSY1 gene produced a strain retaining about 85% of wild type glycogen synthase activity at stationary phase, while disruption of the GSY2 gene yielded a strain with only about 10% of wild type enzyme activity. The level of glycogen synthase activity in yeast cells disrupted for GSY1 increased in stationary phase, whereas the activity remained at a constant low level in cells disrupted for GSY2. Disruption of both genes resulted in a viable haploid that totally lacked glycogen synthase activity and was defective in glycogen deposition. In conclusion, yeast expresses two forms of glycogen synthase with activity levels that behave differently in the growth cycle. The GSY2 gene product appears to be the predominant glycogen synthase with activity linked to nutrient depletion.

Amino Acid Sequence↗

Hepatic glycogen synthesis from duodenal glucose and alanine. An in situ 13C NMR study.

An in situ and in vivo surface coil 13C NMR study was performed to study hepatic glycogen synthesis from [3-13C]alanine and [1-13C]glucose administered by intraduodenal infusion in 18-h fasted male Sprague-Dawley rats. Combined, equimolar amounts of alanine and glucose were given. Hepatic appearance and disappearance of substrate and concurrent glycogen synthesis was followed over 150 min, with 5-min time resolution. Active glycogen synthesis from glucose via the direct (glucose----glycogen) and indirect (glucose----lactate----glycogen) pathways and from alanine via gluconeogenesis was observed. The indirect pathway of glycogen synthesis from [1-13C]glucose accounted for 30% (+/- 6 S.E.) of total glycogen formed from labeled glucose. This estimate does not take into account dilution of label in the hepatic oxaloacetate pool and is, therefore, somewhat uncertain. Hepatic levels of [3-13C]alanine achieved were significantly lower than levels of [1-13C]glucose in the liver, and the period of active glycogen synthesis from [3-13C]alanine was longer than from glucose. However, the overall pseudo-first-order rate constant during the period of active glycogen synthesis from [3-13C]alanine (0.075 min-1 +/- 0.026 S.E.) was almost 3 times that from [1-13C]glucose via the direct pathway (0.025 min-1 +/- 0.005 S.E.). The most likely reason for the small rate constant governing direct glycogen formation from duodenally administered glucose compared to that from duodenally administered alanine is a low level of glucose phosphorylating capacity in the liver.

Alanine↗

Factors affecting changes in muscle glycogen concentration during and after prolonged exercise.

Muscle glycogen concentration decreases continuously during prolonged severe exercise. The rate of depletion increases with increasing exercise intensity. During heavy exercise at 65-75% of VO2 max, time till exhaustion correlates with the pre-exercise muscle glycogen concentration and exhaustion coincides with empty glycogen stores. A substantial number of type I fibres are depleted within 60 min of mild exercise (43% of VO2 max). These results suggest that glycogen depletion may contribute to muscle fatigue even during light exercise. When glycogen depletion becomes present in an increasing number of type I fibres, glycogen breakdown occur in an increasing number of type II fibres, indicating that these fibres take over more of the force development. It is well documented that a high carbohydrate diet is a prerequisite for a rapid post-exercise muscle glycogen resynthesis. Recent studies indicate that there is an increasing rate of glycogen resynthesis with increasing oral glucose intake up to a certain level. A further increase in glucose intake gives no further increase in the rate of resynthesis. However, glucose infusion is reported to induce a 2-3 times higher rate of resynthesis. This higher rate of resynthesis may be caused by the higher blood glucose concentration which can occur during glucose infusion. Preliminary results indicate that muscle glycogen is resynthesized at equal rates when the blood glucose concentration is kept at the same level, irrespective of whether the glucose is administered orally or by infusion. Muscle glycogen resynthesis seems to be slower during fructose ingestion than glucose ingestion.(ABSTRACT TRUNCATED AT 250 WORDS)

Dietary Carbohydrates↗

Comparative purification and characterization of invertebrate muscle glycogen synthase from the porcine parasite Ascaris suum.

Glycogen synthase has been purified from the obliquely striated muscle of the swine parasite Ascaris suum. The muscle contains a concentration of glycogen synthase and glycogen which is 20-fold and 15-fold, respectively, greater than rabbit skeletal muscle. The enzyme could not be solubilized with salivary amylase, but partial solubilization was achieved by activation of endogenous phosphorylase. The enzyme was purified to 85-90% homogeneity (specific activity = 4.3 units/mg) by DEAE-cellulose, Sepharose 4B, and glucosamine 6-phosphate chromatography. The purified glycogen synthase was substantially similar to rabbit skeletal muscle enzyme with respect to Mr (gel electrophoresis and gel filtration), pH dependence, aggregation properties, temperature dependence, and kinetic constants for substrates and activators. Glycogen synthase I was converted to glycogen synthase D by the cyclic AMP-dependent protein kinase. The cyclic AMP-dependent protein kinase catalyzed the incorporation of 1.3 mol of phosphate into each glycogen synthase I subunit and the concomitant interconversion to glycogen synthase D. Since glycogen is the sole fuel utilized by this organism during nonfeeding periods of the host, the characterization of this enzyme provides further insight into the regulatory mechanisms which determine glycogen turnover.

Animals↗

Glycogen in leukocytes from bovine blood and milk.

Glycogen content was determined quantitatively by the Anthrone reagent method in leukocytes obtained from blood and milk of five cows. Distribution of glycogen in leukocytes was studied by microscopic examination of slides stained by Periodic acid-Schiff (PAS) reaction. Blood glucose concentrations were investigated in these animals by standard procedures. In two of five cows both blood glucose levels and blood leukocyte glycogen levels on the same day were determined for six consecutive days. One hundred and two blood leukocyte samples from five cows had a mean glycogen content of 1.32 +/- 0.04 (S.E.) mg/10(9) WBC, and 6.11 +/- 0.17 (S.E.) mg/10(9) PMNs. Leukocyte preparations from 80 samples of milk comprising 97 to 98% PMNs contained 3.81 +/- 0.18 (S.E.) mg glycogen/10(9) milk leukocytes. In PAS preparations of blood and milk leukocytes glycogen was found almost exclusively in PMNs. Glycogen granules, present frequently in PMNs and occasionally in monocytes and large lymphocytes from blood, were not observed in those from milk. The glycogen level in milk leukocytes was significantly lower (P = <0.01) than that of the blood PMNs in every cow, and the overall mean difference between levels for milk leukocytes and blood PMNs was highly significant (P = <0.001). Mean blood glucose concentration in the five cows was 44.46 +/- 0.66 (S.E.) mg%. There was no significant relationship between blood glucose and blood leukocyte glycogen levels in the five corresponding cows; nor between blood glucose and blood PMN glycogen levels on the same day in either of two cows investigated. Leukocyte preparations from milk samples obtained on the second day following intramammary infusion of endotoxin consistently contained markedly less glycogen than the leukocyte preparations from first day post-infusion samples. These tended to level off and became intermediate between first and second day levels. It is postulated that the poor phagocytic competence of leukocytes from bovine mammary glands compared to their counterparts in blood observed by various workers may be due partially to low energy reserves in these cells.

Animals↗