scholarly journals Increase in Subcellular GSK-3 Clusters in Insulin- and Adrenaline-treated Differentiated Rat Skeletal Muscle Fibres

2020 ◽  
Author(s):  
Katja Fink ◽  
Mateja Lobe Prebil ◽  
Nina Vardjan ◽  
Jorgen Jensen ◽  
Robert Zorec ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Metabolic Regulation ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase 3 ◽  
Muscle Fibres ◽  
Optical Section ◽  
Rat Skeletal Muscle ◽  
Average Size ◽  
Skeletal Muscle Fibres

Glycogen synthase kinase 3 (GSK-3) plays an important role in metabolic regulation in skeletal muscles, and both insulin and adrenaline stimulate   GKS-3 phosphorylation. The aim of the present study was to study the effect of insulin and adrenaline on GSK-3 localisation in skeletal muscles.We characterized subcellular localization of (GSK-3) signal protein in fully differentiated muscle fibre by immunofluorescence and confocal microscopy. We stimulated muscle fibres with insulin and/or adrenaline. Images were analysed by segmentation of single central optical section of the muscle.We found GSK-3 to be localised in clusters. The number of GSK-3 clusters and their average size were increased after stimulation with insulin and/or adrenaline. Average GSK-3 particle size is linearly related to their quantity.We conclude that subcellular GSK-3 in isolated skeletal muscle fibres is localized in clusters and clustering increased after stimulation with insulin and/or adrenaline.

Interferon-gamma-like immunoreactivity and T-cell marker expression in rat skeletal muscle fibres

1989 ◽  
Vol 504 (2) ◽  
pp. 306-310 ◽  
Author(s):  
Inger Nennesmo ◽  
Tomas Olsson ◽  
Åke Ljungdahl ◽  
Krister Kristensson ◽  
Peter H. Van der Meide
Keyword(s):  
Skeletal Muscle ◽  
T Cell ◽  
Interferon Gamma ◽  
Muscle Fibres ◽  
Cell Marker ◽  
Rat Skeletal Muscle ◽  
Marker Expression ◽  
Skeletal Muscle Fibres

scholarly journals Extracellular carbonic anhydrase activity facilitates lactic acid transport in rat skeletal muscle fibres

2001 ◽  
Vol 531 (3) ◽  
pp. 743-756 ◽  
Author(s):  
Petra Wetzel ◽  
Anke Hasse ◽  
Simon Papadopoulos ◽  
Juha Voipio ◽  
Kai Kaila ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Lactic Acid ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Muscle Fibres ◽  
Acid Transport ◽  
Rat Skeletal Muscle ◽  
Skeletal Muscle Fibres

scholarly journals Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles

2004 ◽  
Vol 379 (2) ◽  
pp. 505-512 ◽  
Author(s):  
Alessandra NORI ◽  
Elena BORTOLOSO ◽  
Federica FRASSON ◽  
Giorgia VALLE ◽  
Pompeo VOLPE
Keyword(s):  
Skeletal Muscle ◽  
Endoplasmic Reticulum ◽  
Sarcoplasmic Reticulum ◽  
Golgi Complex ◽  
Skeletal Muscles ◽  
Muscle Fibres ◽  
Vesicle Budding ◽  
Er Exit Sites ◽  
Skeletal Muscle Fibres ◽  
Mutant Forms

CS (calsequestrin) is an acidic glycoprotein of the SR (sarcoplasmic reticulum) lumen and plays a crucial role in the storage of Ca2+ and in excitation–contraction coupling of skeletal muscles. CS is synthesized in the ER (endoplasmic reticulum) and is targeted to the TC (terminal cisternae) of SR via mechanisms still largely unknown, but probably involving vesicle transport through the Golgi complex. In the present study, two mutant forms of Sar1 and ARF1 (ADP-ribosylation factor 1) were used to disrupt cargo exit from ER-exit sites and intra-Golgi trafficking in skeletal-muscle fibres respectively. Co-expression of Sar1-H79G (His79→Gly) and recombinant, epitope-tagged CS, CSHA1 (where HA1 stands for nine-amino-acid epitope of the viral haemagglutinin 1), barred segregation of CSHA1 to TC. On the other hand, expression of ARF1-N126I altered the subcellular localization of GM130, a cis-medial Golgi protein in skeletal-muscle fibres and myotubes, without interfering with CSHA1 targeting to either TC or developing SR. Thus active budding from ER-exit sites appears to be involved in CS targeting and routing, but these processes are insensitive to modification of intracellular vesicle trafficking and Golgi complex disruption caused by the mutant ARF1-N126I. It also appears that CS routing from ER to SR does not involve classical secretory pathways through ER–Golgi intermediate compartments, cis-medial Golgi and trans-Golgi network.

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