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

  title={Protein targeting to glycogen mRNA expression is stimulated by noradrenaline in mouse cortical astrocytes},
  author={Igor Allaman and Luc Pellerin and P. J. Magistretti},
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/EBPβ and ‐δ 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… 
A2B receptor activation promotes glycogen synthesis in astrocytes through modulation of gene expression.
Results indicate that adenosine can exert long-term control over glycogen levels in astrocytes and might therefore play a significant role in physiological and/or pathological processes involving long- term modulation of brain energy metabolism.
Glucocorticoids modulate neurotransmitter‐induced glycogen metabolism in cultured cortical astrocytes
The results suggest that GC could have a significant influence on neuroenergetics as they could modulate activity‐related changes in brain glycogen metabolism.
Altered Glycogen Metabolism in Cultured Astrocytes from Mice with Chronic Glutathione Deficit; Relevance for Neuroenergetics in Schizophrenia
Results show that glucose metabolism and glycogen utilization are dysregulated in astrocytes showing a chronic deficit in GSH, suggesting that alterations of a fundamental aspect of brain energy metabolism is caused by GSH deficit and may therefore be relevant to metabolic dysfunctions observed in schizophrenia.
Glycogen Metabolism as a Marker of Astrocyte Differentiation
Results show that glycogen metabolism constitutes a useful marker of astrocyte differentiation.
Structure and Regulation of Glycogen Synthase in the Brain.
Impairments in the glycogen biosynthetic enzymes which lead to glycogen storage diseases in humans are discussed, highlighting effects on the brain and discussing findings in genetically modified animal models that recapitulate these diseases.
Glycogen phosphorylase isozyme pattern in mammalian retinal Müller (glial) cells and in astrocytes of retina and optic nerve
It is shown that Müller cells of rat, rabbit, guinea pig, and mouse retina exclusively express the BB isoform, and astrocytes in the brain and spinal cord as well as the epithelial cells of the pars caeca and of the ciliary body express both the BB and MM isoform.
Astrocyte glycogen and brain energy metabolism
Groundbreaking evidence indicates that astrocyte glycogen offers some protection against hypoglycemic neural injury and ensures that neurons and axons can maintain their function during very intense periods of activation.
Sleep deprivation modulates brain mRNAs encoding genes of glycogen metabolism
Results indicate that expression of genes related to brain glycogen metabolism exhibit variations throughout the sleep‐waking or rest‐activity cycle and given the almost selective localization of glycogen to astrocytes, these cells might participate in the regulation of sleep.
Norepinephrine stimulates glycogenolysis in astrocytes to fuel neurons with lactate
The role of glycogen as a fuel source for neuromodulation using the noradrenergic stimulation of glia in a computational model of the neural-glial-vasculature ensemble (NGV) shows that the energy supply for both astrocytes and neurons can be supplied rapidly by glycogenolysis upon neurmodulatory stimulus.
Activity‐dependent regulation of energy metabolism by astrocytes: An update
Very recent experimental evidence as well as theoretical arguments strongly supporting the original astrocyte‐neuron lactate shuttle concept are reviewed, with new perspectives offered by the application of this concept.


Overexpression of Protein Targeting to Glycogen (PTG) in Rat Hepatocytes Causes Profound Activation of Glycogen Synthesis Independent of Normal Hormone- and Substrate-mediated Regulatory Mechanisms*
Surprisingly, the glycogenic effect of PTG is observed even in the complete absence of carbohydrates or insulin in the culture medium, and this results are consistent with a model in which PTG overexpression “locks” the hepatocyte in a glycogenic mode.
Vasoactive intestinal peptide and noradrenaline exert long-term control on glycogen levels in astrocytes: blockade by protein synthesis inhibition
  • O. SorgP. Magistretti
  • Biology, Chemistry
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1992
This observation, taken together with the fact that dibutyryl-cAMP application also results in enhanced glycogen resynthesis, strongly suggests that the long-term effect of VIP or NA is mediated by the cAMP second-messenger pathway.
Vasoactive intestinal peptide, pituitary adenylate cyclase-activating peptide, and noradrenaline induce the transcription factors CCAAT/enhancer binding protein (C/EBP)-beta and C/EBP delta in mouse cortical astrocytes: involvement in cAMP-regulated glycogen metabolism
The results support the idea that C/EBP beta and -delta regulate gene expression of energy metabolism-related enzymes in astrocytes, and induce the cAMP second-messenger pathway.
L‐Glutamate and Insulin Enhance Glycogen Synthesis in Cultured Astrocytes from the Rat Brain Through Different Intracellular Mechanisms
The results suggest that insulin stimulates glycogen synthesis in astrocytes by activating glycogen synthase, which is dependent on a wortmannin‐sensitive signaling pathway, and L‐Glutamate enhances the glucose uptake, which contributes to the increase in glycogen syntheses in the cells.
PTG, a Protein Phosphatase 1-Binding Protein with a Role in Glycogen Metabolism
Overexpression of PTG markedly increased basal and insulin-stimulated glycogen synthesis in Chinese hamster ovary cells overexpressing the insulin receptor, suggesting that PTG is critical for glycogen metabolism, possibly functioning as a molecular scaffold.