Glycogen phosphorylase isozymes and energy metabolism in the rat peripheral nervous system—An immunocytochemical study

Pfeiffer-Guglielmi, Brigitte; Francke, Mike; Reichenbach, Andreas; Hamprecht, Bernd

doi:10.1016/j.brainres.2006.12.037

Cited by 28 publications

(35 citation statements)

References 41 publications

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“…In the rat brain, GP and glycogen mainly exist in astrocytes, astroglial cells and ependymal cells of ventricles but never in neurons (Pfeiffer-Guglielmi et al, 2003). During energy deprivation in the central nervous system, glycogen is degraded to lactate, which is shuttled from astrocytes to high-energyrequiring neurons (Ransom and Fern, 1997;Brown et al, 2003;Pfeiffer-Guglielmi et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Regulation of glycogen metabolism in gills and liver of the euryhaline tilapia (Oreochromis mossambicus) during acclimation to seawater

Chang

Tseng

et al. 2007

Journal of Experimental Biology

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ATPase activity rapidly increased immediately after SW transfer. Glycogen content in both the gills and liver were significantly depleted after SW transfer, but the depletion occurred earlier in gills than in the liver. Gill GP activity and protein expression were upregulated 1-3·h posttransfer and eventually recovered to the normal level as determined in the control group. At the same time, GS protein expression was downregulated. Similar changes in liver GP and GS protein expression were also observed but they occurred later at 6-12·h post-transfer. In conclusion, GR cells are initially stimulated to provide prompt energy for neighboring MR cells that trigger ion-secretion mechanisms. Several hours later, the liver begins to degrade its glycogen stores for the subsequent energy supply.

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Section: Discussionmentioning

confidence: 99%

Regulation of glycogen metabolism in gills and liver of the euryhaline tilapia (Oreochromis mossambicus) during acclimation to seawater

Chang

Tseng

et al. 2007

Journal of Experimental Biology

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“…In contrast, axons of peripheral nerves express GP BB abundantly, whereas Schwann cells do not contain GP [27,28]. GP MM is primarily activated by phosphorylation triggered by hormones or neurotransmitters.…”

Section: Introductionmentioning

confidence: 87%

Immunohistochemical Localization of Glycogen Phosphorylase Isozymes in the Rat Gastrointestinal Muscle Layers and Enteric Nervous System

et al. 2008

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Glycogen represents the major brain energy reserve though its precise functions are still under debate. Glycogen has also been found in different cell types of the enteric nervous system (ENS), the largest and most complex component of the peripheral nervous system. In the present work we have demonstrated, by application of isozyme-specific antibodies, the presence of isozymes of glycogen phosphorylase (GP), one of the major control sites in glycogen metabolism, in the rat ENS. Immunohistochemistry revealed that isoform BB (brain) is the predominant isozyme expressed in enteric glial cells (EGC) and rare neurons of the myenteric and submucosal plexuses. Isoform MM (muscle) appears in cells which are, according to their location and morphology, probably interstitial cells of Cajal (ICC). In addition, both GP isoforms are expressed in longitudinal and circular intestinal smooth muscle layers. As GP BB is mainly regulated by the cellular AMP level, a special function of glycogen in the energy supply of neural gut functions is suggested.

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“…This, in turn, would lead to mobilization of glucosyl residues of glycogen which are thus channeled into the glycolytic and eventually also the oxidative pathways of energy production. It is likely that GP BB exerts this function not only in the central nervous system [5,30] and the peripheral nervous system [6,31], but also in the heart, another electrically excitable tissue. GP MM, on the other hand, is less sensitive to AMP activation, but-like the other two GP isozymes-is activated by phosphorylation [3].…”

Section: Discussionmentioning

confidence: 99%

“…GP BB is expressed in several types of neural cells, i.e., in astrocytes and ependymal cells of the central and in neurons of the peripheral nervous system [4][5][6]. In non-nervous tissues GP BB has also been detected, with the exception of heart muscle [7] in low concentrations.…”

Section: Introductionmentioning

confidence: 96%

Expression of the Brain and Muscle Isoforms of Glycogen Phosphorylase in Rat Heart

et al. 2008

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Heart glycogen represents a store of glucosyl residues which are mobilized by the catalysis of glycogen phosphorylase (GP) and are mainly destined to serve as substrates for the generation of ATP. The brain isoform of GP (GP BB) was studied in rat heart in comparison with the muscle isoform (GP MM) to find functional analogies to the brain. Western blotting and quantitative reverse transcriptase polymerase chain reaction (RT-PCR) experiments revealed that at the protein level, but not at the mRNA level, the content of GP BB is similar in heart and brain. In contrast, GP MM is more abundant in the heart than in the brain. Immunocytochemically GP BB was colocalized with GP MM in cardiomyocytes. GP MM was also detected in interstitial cells identified as fibroblasts. The physiological role of co-expression of GP BB and GP MM in cardiomyocytes and in brain astrocytes is discussed in a comparative way.

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Glycogen phosphorylase isozymes and energy metabolism in the rat peripheral nervous system—An immunocytochemical study

Cited by 28 publications

References 41 publications

Regulation of glycogen metabolism in gills and liver of the euryhaline tilapia (Oreochromis mossambicus) during acclimation to seawater

Regulation of glycogen metabolism in gills and liver of the euryhaline tilapia (Oreochromis mossambicus) during acclimation to seawater

Immunohistochemical Localization of Glycogen Phosphorylase Isozymes in the Rat Gastrointestinal Muscle Layers and Enteric Nervous System

Expression of the Brain and Muscle Isoforms of Glycogen Phosphorylase in Rat Heart

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