scholarly journals Ca2+leakage out of the sarcoplasmic reticulum is increased in type I skeletal muscle fibres in aged humans

2015 ◽  
Vol 594 (2) ◽  
pp. 469-481 ◽  
Author(s):  
C. R. Lamboley ◽  
V. L. Wyckelsma ◽  
M. J. McKenna ◽  
R. M. Murphy ◽  
G. D. Lamb
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibres ◽  
Type I ◽  
Skeletal Muscle Fibres

scholarly journals Contractile properties and sarcoplasmic reticulum calcium content in type I and type II skeletal muscle fibres in active aged humans

2015 ◽  
Vol 593 (11) ◽  
pp. 2499-2514 ◽  
Author(s):  
C. R. Lamboley ◽  
V. L. Wyckelsma ◽  
T. L. Dutka ◽  
M. J. McKenna ◽  
R. M. Murphy ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Content ◽  
Contractile Properties ◽  
Muscle Fibres ◽  
Type I ◽  
Type Ii ◽  
Skeletal Muscle Fibres ◽  
Sarcoplasmic Reticulum Calcium

Sarcoplasmic reticulum ATPase activity in type I and II skeletal muscle fibres of chronic heart failure patients

2009 ◽  
Vol 133 (2) ◽  
pp. 185-190 ◽  
Author(s):  
Martijn A. Bekedam ◽  
Brechje J. van Beek-Harmsen ◽  
Willem van Mechelen ◽  
Anco Boonstra ◽  
Frans C. Visser ◽  
...  
Keyword(s):  
Heart Failure ◽  
Skeletal Muscle ◽  
Chronic Heart Failure ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Muscle Fibres ◽  
Type I ◽  
Heart Failure Patients ◽  
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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