scholarly journals In vivo Ca2+ dynamics induced by Ca2+ injection in individual rat skeletal muscle fibers

2017 ◽  
Vol 5 (5) ◽  
pp. e13180 ◽  
Author(s):  
Mario Wakizaka ◽  
Hiroaki Eshima ◽  
Yoshinori Tanaka ◽  
Hideki Shirakawa ◽  
David C. Poole ◽  
...  
2000 ◽  
Vol 440 (2) ◽  
pp. 302-308 ◽  
Author(s):  
Tamás Ivanics ◽  
Zsuzsa Miklós ◽  
Zoltán Ruttner ◽  
Sándor Bátkai ◽  
Dick W. Slaaf ◽  
...  

PLoS ONE ◽  
2012 ◽  
Vol 7 (5) ◽  
pp. e35226 ◽  
Author(s):  
Travis L. Dutka ◽  
Esther Verburg ◽  
Noni Larkins ◽  
Kristin H. Hortemo ◽  
Per K. Lunde ◽  
...  

2010 ◽  
Vol 24 (1) ◽  
pp. 88-96 ◽  
Author(s):  
Andreo F Aguiar ◽  
Danilo H Aguiar ◽  
Alan DS Felisberto ◽  
Fernanda R Carani ◽  
Rachel C Milanezi ◽  
...  

Author(s):  
R. B. Armstrong ◽  
C. W. Saubert ◽  
W. L. Sembrowich ◽  
R. E. Shepherd ◽  
P. D. Gollnick

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Shuo Wang ◽  
Bonnie Seaberg ◽  
Ximena Paez-Colasante ◽  
Mendell Rimer

Abstract To test the role of extracellular-signal regulated kinases 1 and 2 (ERK1/2) in slow-twitch, type 1 skeletal muscle fibers, we studied the soleus muscle in mice genetically deficient for myofiber ERK1/2. Young adult mutant soleus was drastically wasted, with highly atrophied type 1 fibers, denervation at most synaptic sites, induction of “fetal” acetylcholine receptor gamma subunit (AChRγ), reduction of “adult” AChRε, and impaired mitochondrial biogenesis and function. In weanlings, fiber morphology and mitochondrial markers were mostly normal, yet AChRγ upregulation and AChRε downregulation were observed. Synaptic sites with fetal AChRs in weanling muscle were ~3% in control and ~40% in mutants, with most of the latter on type 1 fibers. These results suggest that: (1) ERK1/2 are critical for slow-twitch fiber growth; (2) a defective γ/ε-AChR subunit switch, preferentially at synapses on slow fibers, precedes wasting of mutant soleus; (3) denervation is likely to drive this wasting, and (4) the neuromuscular synapse is a primary subcellular target for muscle ERK1/2 function in vivo.


1970 ◽  
Vol 29 (1) ◽  
pp. 142-151 ◽  
Author(s):  
Edward R. Chaplin ◽  
George W. Nell ◽  
Sheppard M. Walker

2000 ◽  
Vol 278 (1) ◽  
pp. C126-C135 ◽  
Author(s):  
Adrian M. Duke ◽  
Derek S. Steele

The effects of Pi on sarcoplasmic reticulum (SR) Ca2+ regulation were studied in mechanically skinned rat skeletal muscle fibers. Brief application of caffeine was used to assess the SR Ca2+ content, and changes in concentration of Ca2+([Ca2+]) within the cytosol were detected with fura 2 fluorescence. Introduction of Pi (1–40 mM) induced a concentration-dependent Ca2+ efflux from the SR. In solutions lacking creatine phosphate (CP), the amplitude of the Pi-induced Ca2+ transient approximately doubled. A similar potentiation of Pi-induced Ca2+ release occurred after inhibition of creatine kinase (CK) with 2,4-dinitrofluorobenzene. In the presence of ruthenium red or ryanodine, caffeine-induced Ca2+ release was almost abolished, whereas Pi-induced Ca2+ release was unaffected. However, introduction of the SR Ca2+ ATPase inhibitor cyclopiazonic acid effectively abolished Pi-induced Ca2+ release. These data suggest that Pi induces Ca2+ release from the SR by reversal of the SR Ca2+ pump but not via the SR Ca2+ channel under these conditions. If this occurs in intact skeletal muscle during fatigue, activation of a Ca2+efflux pathway by Pi may contribute to the reported decrease in net Ca2+ uptake and increase in resting [Ca2+].


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