Suppression of glycogen storage with betamethasone 17,21-dipropionate in fetal rat liver--I. Effect on metabolites of the glucogenic pathway and glycogen synthase activity.

doi:10.1016/0006-2952(79)90351-4

Paper

Suppression of glycogen storage with betamethasone 17,21-dipropionate in fetal rat liver--I. Effect on metabolites of the glucogenic pathway and glycogen synthase activity.

Published Mar 15, 1979 · Y. Mizushima, M. Ishikawa, Y. Hasegawa

Biochemical pharmacology

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Abstract

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Non-RCT

Animal Study

Study Snapshot

Betamethasone 17,21-dipropionate suppresses glycogen accumulation in fetal rat liver during late pregnancy, with inhibition between UDP-glucose and glycogen playing a key role in this action.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Suppression of glycogen storage with betamethasone 17,21-dipropionate in fetal rat liver--I. Effect on metabolites of the glucogenic pathway and glycogen synthase activity.

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References

The role of glucocorticoids in the regulation of glucose-6-phosphatase activity in fetal rat liver.

Glucocorticoids play a crucial role in regulating glucose-6-phosphatase activity in fetal rat liver during late pregnancy by modulating the action of cAMP.

Suppression of glycogen storage with betamethasone 17,21-dipropionate in fetal rat liver--II. Inhibition of glycogenic action of cortisol and insulin in the liver in organ culture.

Betamethasone 17,21-dipropionate effectively suppresses the glycogenic actions of cortisol and partially suppresses insulin-induced glycogen accumulation in fetal rat liver in organ culture.

Glycogen metabolism in the liver of the developing rat.

The ratio of phosphorylase a/synthase I and glycogen content in the liver is closely related to the development of glycogen metabolism in the developing rat.

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

Cortisol is necessary for the glycogenic effect of insulin in fetal hepatocyte culture, but not necessary for the glucagon-dependent regulatory pathway in fetal development.

Effect of hydrocortisone and glucagon on glycogen metabolism in the fetal rat liver.

Hydrocortisone increases glycogen incorporation in fetal liver glycogen during the last days of gestation, while glucagon slightly decreases it, with no significant effect on synthetase a or total synthetase activity.

Citations

Increased Phospholipid Methylation and Glycogen Phosphorylase Activation after a Single Dose of Dexamethasone in Mouse Liver

Dexamethasone treatment in mice livers increases phospholipid methylation and activates glycogen phosphorylase a, with biphasic effects on glycogen phosphorylase a activity.

An effect of dexamethasone on glycogen metabolism in hepatocyte cultures

Dexamethasone effectively regulates hepatic glycogen metabolism in hepatocyte cultures, providing a useful system for studying glucocorticoid effects on glycogen metabolism.

The role of glucocorticoids in the regulation of glucose-6-phosphatase activity in fetal rat liver.

Glucocorticoids play a crucial role in regulating glucose-6-phosphatase activity in fetal rat liver during late pregnancy by modulating the action of cAMP.

Suppression of glycogen storage with betamethasone 17,21-dipropionate in fetal rat liver--II. Inhibition of glycogenic action of cortisol and insulin in the liver in organ culture.

Betamethasone 17,21-dipropionate effectively suppresses the glycogenic actions of cortisol and partially suppresses insulin-induced glycogen accumulation in fetal rat liver in organ culture.