Adrenaline and glycogen synthase activity in fast and slow muscles of rat

Moruzzi, E. Villa; Cubeddu, Tiziana; Bergamini, Ettore

doi:10.1016/0014-5793(80)80827-1

Cited by 6 publications

(7 citation statements)

References 12 publications

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“…2001). Moruzzi et al. (1980) demonstrated that the recovery of total GS activity (a measure of GS protein content) in myofibrillar sediments increased in response to adrenaline administration in vivo and our experiments indicate that this is most likely due to the glycogen‐depleting action of adrenaline (Nielsen et al.…”

Section: Muscle Glycogen Contentmentioning

confidence: 56%

“…Furthermore, GS protein content of a 2700 g pellet in fast-twitch muscle increased when glycogen was low but this was not the case in the slow-twitch soleus muscle . Moruzzi et al (1980) were also able to show an effect of adrenaline on GS translocation in fast but not in slow-twitch muscle, suggesting that GS translocation to the cytoskeleton is muscle fibre-type specific.…”

Section: Muscle Glycogen Contentmentioning

confidence: 89%

“…2001). Moruzzi et al. (1980) were also able to show an effect of adrenaline on GS translocation in fast but not in slow‐twitch muscle, suggesting that GS translocation to the cytoskeleton is muscle fibre‐type specific.…”

Section: Muscle Glycogen Contentmentioning

confidence: 93%

“…Therefore, extrapolation of results concerning GS and related enzymes from nonmuscle cell types to the regulation of GS in skeletal muscle should be done cautiously. In skeletal muscle it has been demonstrated that GS is associated with glycogen particles (Meyer et al 1970, Bergamini et al 1977 but also with myofibrils (Moruzzi et al 1980, Lane et al 1989. Moruzzi et al (1980) demonstrated that the recovery of total GS activity (a measure of GS protein content) in myofibrillar sediments increased in response to adrenaline administration in vivo and our experiments indicate that this is most likely due to the glycogen-depleting action of adrenaline ).…”

Section: Muscle Glycogen Contentmentioning

confidence: 99%

“…In skeletal muscle it has been demonstrated that GS is associated with glycogen particles (Meyer et al 1970, Bergamini et al 1977 but also with myofibrils (Moruzzi et al 1980, Lane et al 1989. Moruzzi et al (1980) demonstrated that the recovery of total GS activity (a measure of GS protein content) in myofibrillar sediments increased in response to adrenaline administration in vivo and our experiments indicate that this is most likely due to the glycogen-depleting action of adrenaline ). In the latter study, it was also demonstrated in fast-twitch muscle that some GS translocates from the glycogen-enriched fraction to the cytoskeleton when glycogen content in skeletal muscle decreases.…”

Section: Muscle Glycogen Contentmentioning

confidence: 99%

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Regulation of glycogen synthase in skeletal muscle during exercise

Nielsen

Richter

2003

Acta Physiologica Scandinavica

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Glycogen synthase (GS) catalyses the incorporation of uridine diphosphate-glucose into glycogen in skeletal muscle. In concert with the glucose transport step, GS activity is thought to be rate-limiting in the disposal of glucose as muscle glycogen. Glycogen synthase is regulated by both allosteric factors (primarily glucose 6-phosphate) and covalent modification by reversible phosphorylation and dephosphorylation leading to inactivation and activation of GS, respectively. Exercise activates both stimulatory and inhibitory regulators of GS and it is thought that the resultant activity of GS during exercise depends on the relative strength of opposing signals. However, the mechanisms by which exercise regulates GS activity are not fully understood. Glycogen breakdown, the GM-protein phosphatase 1 complex and possibly cellular relocalization of GS may be considered important factors involved in the stimulation of GS activity during exercise, while adenosine monophosphate-activated protein kinase and plasma adrenaline (via protein kinase A) can be considered as essential for the exercise-induced inhibitory signals to GS.

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Section: Muscle Glycogen Contentmentioning

confidence: 56%

Section: Muscle Glycogen Contentmentioning

confidence: 89%

Section: Muscle Glycogen Contentmentioning

confidence: 93%

Section: Muscle Glycogen Contentmentioning

confidence: 99%

Section: Muscle Glycogen Contentmentioning

confidence: 99%

See 3 more Smart Citations

Regulation of glycogen synthase in skeletal muscle during exercise

Nielsen

Richter

2003

Acta Physiologica Scandinavica

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Effects of PCB on the adrenergic response in perfused gills and on levels of muscle glycogen in Rainbow trout (Salmo gairdneri Rich.)

Kiessling

Pärt

Ring

et al. 1983

Bull. Environ. Contam. Toxicol.

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Glycogen synthase localization and activity in rat skeletal muscle is strongly dependent on glycogen content

Nielsen

Derave

Kristiansen

et al. 2001

The Journal of Physiology

119

125

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1. The influence of muscle glycogen content on glycogen synthase (GS) localization and GS activity was investigated in skeletal muscle from male Wistar rats.2. Two groups of rats were obtained, preconditioned with a combination of exercise and diet to obtain either high (HG) or low (LG) muscle glycogen content. The cellular distribution of GS was studied using subcellular fractionation and confocal microscopy of immunostained single muscle fibres. Stimulation of GS activity in HG and LG muscle was obtained with insulin or contractions in the perfused rat hindlimb model.3. We demonstrate that GS translocates from a glycogen-enriched membrane fraction to a cytoskeleton fraction when glycogen levels are decreased. Confocal microscopy supports the biochemical observations that the subcellular localization of GS is influenced by muscle glycogen content. GS was not found in the nucleus.4. Investigation of the effect of glycogen content on GS activity in basal and insulin-and contraction-stimulated muscle shows that glycogen has a strong inhibitory effect on GS activity. Our data demonstrate that glycogen is a more potent regulator of glycogen synthase activity than insulin. Furthermore we show that the contraction-induced increase in GS activity is merely a result of a decrease in muscle glycogen content.5. In conclusion, the present study shows that GS localization is influenced by muscle glycogen content and that not only basal but also insulin-and contraction-stimulated GS activity is strongly regulated by glycogen content in skeletal muscle.

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Adrenaline and glycogen synthase activity in fast and slow muscles of rat

Cited by 6 publications

References 12 publications

Regulation of glycogen synthase in skeletal muscle during exercise

Regulation of glycogen synthase in skeletal muscle during exercise

Effects of PCB on the adrenergic response in perfused gills and on levels of muscle glycogen in Rainbow trout (Salmo gairdneri Rich.)

Glycogen synthase localization and activity in rat skeletal muscle is strongly dependent on glycogen content

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