scholarly journals Enhancing effect of calmodulin on Ca(2+)-induced Ca2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres.

1995 ◽  
Vol 487 (3) ◽  
pp. 573-582 ◽  
Author(s):  
T Ikemoto ◽  
M Iino ◽  
M Endo
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Rabbit Skeletal Muscle ◽  
Muscle Fibres ◽  
Enhancing Effect ◽  
Skeletal Muscle Fibres

Further histochemical properties of rabbit skeletal muscle fibres

1973 ◽  
Vol 36 (2) ◽  
pp. 173-183 ◽  
Author(s):  
M. A. Khan ◽  
J. M. Papadimitriou ◽  
P. G. Holt ◽  
B. A. Kakulas
Keyword(s):  
Skeletal Muscle ◽  
Rabbit 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 Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres

2007 ◽  
Vol 579 (2) ◽  
pp. 313-326 ◽  
Author(s):  
Alicia Moreno-Gonzalez ◽  
Todd E. Gillis ◽  
Anthony J. Rivera ◽  
P. Bryant Chase ◽  
Donald A. Martyn ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Rabbit Skeletal Muscle ◽  
Muscle Fibres ◽  
Thin Filament Regulation ◽  
Skeletal Muscle Fibres
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