scholarly journals Role of calsequestrin evaluated from changes in free and total calcium concentrations in the sarcoplasmic reticulum of frog cut skeletal muscle fibres

2007 ◽  
Vol 581 (1) ◽  
pp. 319-367 ◽  
Author(s):  
Paul C. Pape ◽  
Karine Fénelon ◽  
Cédric R. H. Lamboley ◽  
Dorothy Stachura
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibres ◽  
Total Calcium ◽  
Skeletal Muscle Fibres

The role of agrin during the maturation of human skeletal muscle fibres

2006 ◽  
Vol 99 (2-3) ◽  
pp. 1
Author(s):  
Fabio Ruzzier ◽  
Elena Bandi ◽  
Mihaela Jurdana ◽  
Paola Lorenzon ◽  
Marina Sciancalepore
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Muscle Fibres ◽  
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.

scholarly journals Sarcoplasmic reticulum Ca2+ depletion in adult skeletal muscle fibres measured with the biosensor D1ER

2010 ◽  
Vol 459 (5) ◽  
pp. 725-735 ◽  
Author(s):  
Ramón Jiménez-Moreno ◽  
Zhong-Ming Wang ◽  
María Laura Messi ◽  
Osvaldo Delbono
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibres ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibres
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