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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

The anaerobic glycogen consumption and the question of post-anaerobic glycogen resynthesis in some invertebrates

Cleary, Mary Baptist, January 1948 (has links)
Thesis--Catholic Univ. of America. / "Literature cited": p. 17-18.
2

A chemical study of glycogen and its preparation ...

McBride, James Joseph, January 1929 (has links)
Thesis (PH. D.)--Columbia University, 1930. / Vita. Bibliography: p. [29].
3

Ein beitrag zur physiologie des glykogens ...

Adamoff, Wera. January 1904 (has links)
Innaug.-Diss.--Bern.
4

Glucocorticoid and its effect on cardiac glucose utilization

Puthanveetil, Prasanth Nair 11 1900 (has links)
Glycogen is an immediate source of glucose for cardiac tissue to maintain its metabolic homeostasis. However, its excess brings about cardiac structural and physiological impairments. Previously, we have demonstrated that in hearts from dexamethasone (DEX) treated animals, glycogen accumulation was enhanced. We examined the influence of DEX on glucose entry and glycogen synthase as a means of regulating the accumulation of this stored polysaccharide. Following DEX, cardiac tissue had limited contribution towards the development of whole body insulin resistance. Measurement of GLUT4 at the plasma membrane revealed an excess presence of this transporter protein at this location. Interestingly, this was accompanied by an increase in GLUT4 in the intracellular membrane fraction, an effect that was well correlated to an increased GLUT4 mR.NA. Both total and phosphorylated AMPK increased following DEX. Immunoprecipitation of AS 160 followed by Western blotting demonstrated no change in Akt phosphorylation at Ser473 and Thr308 in DEX treated hearts. However, there was a significant increase in AMPK phosphorylation at Thr172, which correlated well with AS 160 phosphorylation. In DEX hearts, there was a considerable reduction in the phosphorylation of glycogen synthase, whereas GSK-3-β phosphorylation was augmented. Our data suggest that AMPK mediated glucose entry, combined with activation of glycogen synthase and reduction in glucose oxidation (Qi, D., et al. Diabetes 53:1790, 2004), act together to promote glycogen storage. Our data suggest that in the presence of intact insulin signaling, AMPK mediated glucose entry, combined with activation of glycogen synthase and the previously reported reduction in glucose oxidation, act together to promote glycogen storage. Should these effects persist chronically, they may explain the increased morbidity and mortality observed with long term excesses in endogenous or exogenous glucocorticoids.
5

Glucocorticoid and its effect on cardiac glucose utilization

Puthanveetil, Prasanth Nair 11 1900 (has links)
Glycogen is an immediate source of glucose for cardiac tissue to maintain its metabolic homeostasis. However, its excess brings about cardiac structural and physiological impairments. Previously, we have demonstrated that in hearts from dexamethasone (DEX) treated animals, glycogen accumulation was enhanced. We examined the influence of DEX on glucose entry and glycogen synthase as a means of regulating the accumulation of this stored polysaccharide. Following DEX, cardiac tissue had limited contribution towards the development of whole body insulin resistance. Measurement of GLUT4 at the plasma membrane revealed an excess presence of this transporter protein at this location. Interestingly, this was accompanied by an increase in GLUT4 in the intracellular membrane fraction, an effect that was well correlated to an increased GLUT4 mR.NA. Both total and phosphorylated AMPK increased following DEX. Immunoprecipitation of AS 160 followed by Western blotting demonstrated no change in Akt phosphorylation at Ser473 and Thr308 in DEX treated hearts. However, there was a significant increase in AMPK phosphorylation at Thr172, which correlated well with AS 160 phosphorylation. In DEX hearts, there was a considerable reduction in the phosphorylation of glycogen synthase, whereas GSK-3-β phosphorylation was augmented. Our data suggest that AMPK mediated glucose entry, combined with activation of glycogen synthase and reduction in glucose oxidation (Qi, D., et al. Diabetes 53:1790, 2004), act together to promote glycogen storage. Our data suggest that in the presence of intact insulin signaling, AMPK mediated glucose entry, combined with activation of glycogen synthase and the previously reported reduction in glucose oxidation, act together to promote glycogen storage. Should these effects persist chronically, they may explain the increased morbidity and mortality observed with long term excesses in endogenous or exogenous glucocorticoids.
6

Crystallographic studies on phosphorylase : sugar recognition properties

Watson, Kimberly Ann January 1994 (has links)
No description available.
7

The role of glycogen synthase kinase 3-beta in interferon beta biology /

Wang, Huizhi, January 2009 (has links) (PDF)
Thesis (Ph. D.)--University of Louisville, 2009. / Department of Microbiology and Immunology. Vita. "May 2009." Includes bibliographical references (leaves 64-76).
8

Glycogen resynthesis following submaximal and supramasimal exhaustive exercise in man

Okocha, Augustine Emefiene. January 1984 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1984. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 109-119).
9

Studies on glycogen phosphorylase

Gilgan, Michael Wilson January 1962 (has links)
PART I GLYCOGEN PHOSPHORYLASE IN BRAIN, ILEUM AND UTERUS In recent years considerable attention has been devoted to the nature of the glycogen phosphorylase enzyme system in skeletal muscle, cardiac muscle and liver. It has been established that those factors which affect the action of this enzyme constitute a major metabolic control mechanism. Considerably less attention has been paid to this enzyme system in tissues which are known to contain low glycogen, stores. The present study constitutes a preliminary examination of glycogen phosphorylase in brain, uterus and ileum. It has been found that brain contains considerably higher phosphorylase activity than liver and is comparable to heart. Uterus and ileum contain enzyme levels comparable to that of liver. The data suggests that the enzyme exists in two forms in these three tissues, one active in the presence of adenosine-5'-monophosphate, the other active in the absence of this nucleotide. The enzyme in each tissue is thus very similar to the skeletal muscle enzyme, but different from that in liver. Preliminary evidence was also obtained which indicates that phosphorylase activating and inactivating enzymes were present. Levels of active phosphorylase were increased in brain and uterus in the presence of epinephrine. The intestinal smooth muscle enzyme failed to respond to epinephrine. The evidence, although preliminary, is consistent with the idea that catecholamine-induced muscle contraction is associated with phosphorylase activation. PART II SYNTHESIS AND ENZYMATIC DEGRADATION OF SEVERAL DE0XYRIB0NUCLE0SIDE-3',5’-MONOPHOSPHATES It is known, that the phosphorylase activating action of epinephrine is mediated through adenosine-3',5'-monophosphate. The metabolism of this important nucleotide is attracting widespread attention. In order to study its seemingly manifold actions, the need has arisen for structural analogues of the compound. Several ribonucleoside-3',5'-monophosphates have already been prepared. In the present work several deoxyribonucleoside-3’,5'-monophosphates were synthesized. These included the nucleoside-3’,5'-monophosphates of deoxyadenosine, deoxyinosine, and deoxyuridine. These compounds were shown to be hydrolysed by a phosphodiesterase from brain which is specific for nucleoside-3',5'-monophosphates. The product of the hydrolysis, in each case, was identified as the corresponding deoxyribonucleoside-5'-phosphate. / Medicine, Faculty of / Anesthesiology, Pharmacology and Therapeutics, Department of / Graduate
10

Glucocorticoid and its effect on cardiac glucose utilization

Puthanveetil, Prasanth Nair 11 1900 (has links)
Glycogen is an immediate source of glucose for cardiac tissue to maintain its metabolic homeostasis. However, its excess brings about cardiac structural and physiological impairments. Previously, we have demonstrated that in hearts from dexamethasone (DEX) treated animals, glycogen accumulation was enhanced. We examined the influence of DEX on glucose entry and glycogen synthase as a means of regulating the accumulation of this stored polysaccharide. Following DEX, cardiac tissue had limited contribution towards the development of whole body insulin resistance. Measurement of GLUT4 at the plasma membrane revealed an excess presence of this transporter protein at this location. Interestingly, this was accompanied by an increase in GLUT4 in the intracellular membrane fraction, an effect that was well correlated to an increased GLUT4 mR.NA. Both total and phosphorylated AMPK increased following DEX. Immunoprecipitation of AS 160 followed by Western blotting demonstrated no change in Akt phosphorylation at Ser473 and Thr308 in DEX treated hearts. However, there was a significant increase in AMPK phosphorylation at Thr172, which correlated well with AS 160 phosphorylation. In DEX hearts, there was a considerable reduction in the phosphorylation of glycogen synthase, whereas GSK-3-β phosphorylation was augmented. Our data suggest that AMPK mediated glucose entry, combined with activation of glycogen synthase and reduction in glucose oxidation (Qi, D., et al. Diabetes 53:1790, 2004), act together to promote glycogen storage. Our data suggest that in the presence of intact insulin signaling, AMPK mediated glucose entry, combined with activation of glycogen synthase and the previously reported reduction in glucose oxidation, act together to promote glycogen storage. Should these effects persist chronically, they may explain the increased morbidity and mortality observed with long term excesses in endogenous or exogenous glucocorticoids. / Pharmaceutical Sciences, Faculty of / Graduate

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