Glycogen metabolism in the developing accessory lobes of Lachi in the nerve cord of the chick: metabolic correlations with the avian glycogen body

Glycogen synthase, glycogen phosphorylase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glucose-6-phosphatase were determined for the first time in the necessary lobes of Lachi from late embryonic chicks. The activities of these enzymes were compared with those found in other glycogen-metabolizing tissues, specifically the glycogen body, liver, and skeletal muscle, obtained from the same embryos. The data show that, as in the glycogen body, the accessory lobes of Lachi lack glucose-6-phosphatase, but contain relatively high activity levels of glycogen synthase I, total and active glycogen phosphorylase, and the dehydrogenases of glucose-6-phosphate and 6-phosphogluconate. The percent of glycogen synthase I activity in the Lachi lobes is from two- to 20-fold greater than observed in the glycogen body, liver, or muscle, whereas the percent of glycogen phosphorylase a activity is comparable to that of the liver, but greater than that in the glycogen body or muscle. The activity of each dehydrogenase of the pentose phosphate cycle in the Lachi lobes is similar to that noted in the glycogen body, but is over two- or fivefold greater than that activity found in muscle or liver. Our data, together with other recent evidence, suggest that the role of glycogen in these functionally enigmatic tissues may be to support the precocious process of myelin synthesis in the developing bird, as well as possibly to provide alternate sources of energy for the avian central nervous system.     

Glycogen metabolic enzymes in the skeletal muscles of the developing chick embryo

In the skeletal muscles of the chick embryo from the 10th till the 15th day of embryogenesis, phosphorylase (EC. 2.4.1.1) is represented by two isozymes one of which corresponds, by electrophoretic mobility, to the liver phosphorylase and another to phosphorylase of the skeletal muscles of the adult rat. From the 17th day of embryogenesis on only one isozyme of phosphorylase is found in the skeletal muscles which is identical with that of the skeletal muscles of the adult bird. The isozyme spectrum of phosphorylase of the whole 4 days old embryo contains, besides phosphorylase L, a special "embryonic" isozyme which differs from that of the skeletal muscles by immunochemical characteristics and electrophoretic mobility. From the 10th day of embryogenesis till hatching, the activity of phosphorylase of the skeletal muscles increases more than 50 times and that of glycogen synthetase (EC. 2.4.1.11) only 4 times.     

The blood-brain barrier of the chick glycogen body (corpus gelatinosum) and its functional implications

Among recent vertebrates only birds possess a glycogen body (corpus gelatinosum), located in the rhomboidal sinus of the lumbosacral region of the spinal cord and separated from the neural tissue proper. Because of the specific topographical situation of this circumventricular organ, the structure of its vascular system is of special interest with respect to the still unsolved functional problems. The existence of a blood-brain barrier is demonstrated by the exclusion of intravascularly injected tracer (horseradish peroxidase), and immunocytochemical demonstration of glucose transporter-1 as a functional marker and of neurothelin, occludin and ZO-1 as structural markers. Alkaline phosphatase and gamma-glutamyltransferase activities, two enzyme reactions frequently used for demonstration of an established blood-brain barrier in vitro, were localized histochemically on the plasmalemma of glycogen body cells and were absent from the endothelium. In addition, local enlargements of the intercellular space were observed by transmission and scanning electron microscopy. In accordance with the concept of a third circulation the cerebrospinal fluid may be the vehicle for distributing substances originating in the glycogen body to the CNS, while the vascular endothelium maintains the internal milieu by virtue of its dynamic barrier functions.     

Glycogen metabolism in the prelaid chick embryo.

Glycogen metabolism has been studied during the development of the early chick embryo, at the cytochemical and ultrastructural levels. Two waves of glycogen synthesis and breakdown have been found. In the first, free clusters of glycogen particles are synthesized at late oogenesis. These clusters are found later in invaginations of the membrane of vesicles containing a floccular material (FLOV). The glycogen clusters are degraded there during ovulation and the first hours in the oviduct. The second wave of glycogen synthesis begins before cleavage, reaching a maximum at mid-uterine age. This second wave occurs in another type of vesicle (GLYV), which eventually disintegrates releasing free clusters of glycogen granules. This glycogen is degraded in membranous structures containing a floccular material, as in the first wave of degradation. The degradation ends at the late uterine stages, and at the same time numerous ribosomes are formed. This period corresponds to area pellucida formation, which probably depends on the energy liberated during the second wave of glycogen degradation.     

Glycogen debranching pathway deduced from substrate specificity of glycogen debranching enzyme

Glycoconjugate Journal - Glycogen debranching enzyme (GDE) is bifunctional in that it exhibits both 4-α-glucanotransferase and amylo-α-1,6-glucosidase activity at two distinct catalytic...     

The pentose phosphate pathway in developing chick cornea

Embryonic chick corneas at different stages of development were evaluated for activity of the pentose phosphate pathway. The appearance of activity was concurrent with the onset of corneal transperancy (stage 40). Highest values were found after complete transparency is achieved (stage 45 and after hatching). Phenazine methosulfate, an artificial electron acceptor, increased activity at all stages studied even before endogenous activity was measurable; however, no increase in glucose uptake was observed. Thus, the enzymes for the pathway are present at early stages (i.e., stage 38 and 40) although in latent form. The pathway probably functions in the developing cornea to generate NADPH rather than sugar moieties for macromolecular incorporation.     

Glycogen biosynthesis in Chromatium strain D: I. Characterization of glycogen

Glycogen granules were isolated from the photosynthesizing cellsof purple sulfur bacterium, Chromatium strain D, and the chemicalstructure was studied by enzymic hydrolysis using -and ß-amylasesand pullulanase. The end-group assay of the bacterial glycogenby periodate oxidation gave the following analytical data: (average chain length), 11; ICL (interiorchain length), 3; and ECL (exterior chain length), 7. We concludethat the Chromatium glycogen is a glycogen- and amylopectin-type-glucan. Intracellular accumulation of glycogen granules inthe bacterial cells harvested at different growth stages wasexamined by electron microscope observation. ¹This research was supported in part by a research grant fromthe Ministry of Education of Japan (No. 758036). (Received February 9, 1973; )     

Pseudomonas cepacia mutants blocked in the direct oxidative pathway of glucose degradation.

Glucose dehydrogenase-deficient strains of Pseudomonas cepacia grew normally with glucose as carbon source, indicating that the direct pathway of glucose oxidation does not play an essential role in this bacterium.     

Activities of the enzymes of ketone body metabolism in the developing chick

The concentration of ketone bodies in the blood of the developing chick prior to and just after hatching were higher than those found in the adult. The activities of 3-oxo acid-CoA transferase and acetoacetyl-CoA thiolase in the heart, leg and pectoral muscle before and after hatching were higher than those of the adult. The activity of 3-hydroxybutyrate dehydrogenase increased constantly during incubation and after hatching in all three muscle tissues. In the liver the activities of the enzymes of ketone body synthesis increased during incubation and after hatching. It is suggested that the liver could provide fuel to the extrahepatic tissues of the developing chick and ketone bodies could contribute as fuel for oxidation in the skeletal muscle of the newly hatched bird.     

Glycogen metabolism in the liver of the developing rat.

1. The total activity of glycogen synthease increased 20-fold from day 17 of gestation to birth at day 22, with a further increase of 18% in the 24h after birth. Active synthase (I) rose 45-fold to a maximum at day 21, fell 40% before birth, and then increased by a similar amount 24h after birth. The fraction of synthase in the active form correlated very well with the deposition of glycogen in the liver. 2. Total phosphorylase had a similar developmental pattern of total synthease with an 18-fold increase from day 17 to day 22. The appearance of active phosphorylase showed a lag-period compared with total phosphorylase and did not increase significantly until day 20. The fraction of phosphorylase in the active form did not correlate at all with glycogen deposition or mobilization. 3. There was a close relationshp between the ratio of phosphorylase a/synthase I and the glycogen content of the liver. An increase or decrease in this ratio would result in glycogenolysis of glycogenesis respectively. 4. It is postulated that a cycle between the two enzymes under basal conditions could exist which permits a continuous turnover of glycogen. Such a system would explain why active phosphorylase is always seen, even under conditions of net glycogen synthesis. The differences in hormone sensitivity of synthase and phosphorylase would also be accounted for as only one enzyme would have to respond acutely to hormonal influences.     

Ultrastructural and biochemical evidence of glycogen in the developing lung of the chick embryo: possible contribution to surfactant

1. Glycogen was identified ultrastructurally in undifferentiated type-II cells of the lung of the day 16 chick embryo. 2. By 4 days after hatching, glycogen in type-II cells could not be observed, although lungs were actively secreting surfactant. 3. Biochemical measurements of pulmonary glycogen revealed a depletion during days 14-20 of incubation, corroborating ultrastructural data. 4. Using lung slices, 14C-glucose was incorporated in vitro into pulmonary surfactant phospholipids at a high rate in day 14 embryos, and a significantly lower rate on day 19. 5. Hypophysectomy resulted in sub-normal initial accumulation of pulmonary glycogen on day 14 of development, but did not alter the depletion pattern after day 16. 6. Thus, glycogen stores may contribute to avian embryonic pulmonary surfactant, and accumulation of early stores may be under hormonal control.