scholarly journals Excitable properties of adult skeletal muscle fibres from the honeybee Apis mellifera

2007 ◽  
Vol 210 (3) ◽  
pp. 454-464 ◽  
Author(s):  
C. Collet ◽  
L. Belzunces
Keyword(s):  
Skeletal Muscle ◽  
Apis Mellifera ◽  
Muscle Fibres ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibres

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

scholarly journals Constitutive Expression of Yes-Associated Protein (Yap) in Adult Skeletal Muscle Fibres Induces Muscle Atrophy and Myopathy

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e59622 ◽  
Author(s):  
Robert N. Judson ◽  
Stuart R. Gray ◽  
Claire Walker ◽  
Andrew M. Carroll ◽  
Cecile Itzstein ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Constitutive Expression ◽  
Muscle Fibres ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibres

scholarly journals Functional role of store-operated and stretch-activated channels in murine adult skeletal muscle fibres

2006 ◽  
Vol 575 (3) ◽  
pp. 913-924 ◽  
Author(s):  
Thomas Ducret ◽  
Clarisse Vandebrouck ◽  
My Linh Cao ◽  
Jean Lebacq ◽  
Philippe Gailly
Keyword(s):  
Skeletal Muscle ◽  
Functional Role ◽  
Muscle Fibres ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibres ◽  
Stretch Activated Channels

scholarly journals Quantitative reduction of RyR1 protein caused by a single-allele frameshift mutation in RYR1 ex36 impairs the strength of adult skeletal muscle fibres

2019 ◽  
Vol 28 (11) ◽  
pp. 1872-1884 ◽  
Author(s):  
Moran Elbaz ◽  
Alexis Ruiz ◽  
Jan Eckhardt ◽  
Pawel Pelczar ◽  
Francesco Muntoni ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Frameshift Mutation ◽  
Muscle Fibres ◽  
Adult Skeletal Muscle ◽  
Single Allele ◽  
Skeletal Muscle Fibres

scholarly journals Cytoskeleton-extracellular matrix interaction is required to maintain mitochondrial Ca2+ control in mouse skeletal muscle fibre

2021 ◽  
Author(s):  
Charlotte Gineste ◽  
Sara Henriksson ◽  
Andres Hernandez ◽  
Arthur J Cheng ◽  
Thomas Chaillou ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Matrix Protein ◽  
Skeletal Muscle Fibre ◽  
Mitochondrial Morphology ◽  
Muscle Fibres ◽  
Cyclophilin D ◽  
Adult Skeletal Muscle ◽  
Mouse Skeletal Muscle ◽  
Skeletal Muscle Fibres

Cells rapidly lose their physiological phenotype upon isolation from their native microenvironment. Here, we investigated the role of the extracellular matrix (ECM) for mitochondrial morphology and Ca2+ handling in adult mouse skeletal muscle fibres. Adult skeletal muscle fibres were isolated from mouse toe muscle either by collagenase-induced dissociation of the ECM or by mechanical dissection that leaves the proximate ECM intact. Experiments were generally performed four hours after cell isolation. At this time, the expression of genes encoding for structural proteins was lower in enzymatically dissociated than in mechanically dissected fibres. Mitochondrial appearance was grossly similar in the two groups, but 3D electron microscopy revealed shorter and less branched mitochondria in enzymatically dissociated than in mechanically dissected fibres. The increase in free cytosolic [Ca2+] during repeated tetanic stimulation was similar in the two groups of fibres, but this was accompanied by an excessive mitochondrial Ca2+ uptake only in enzymatically dissociated muscle fibres. The aberrant mitochondrial Ca2+ uptake was partially prevented by the mitochondrial Ca2+ uniporter inhibitor Ru360 and by cyclosporine A and NV556, which inhibit the mitochondrial matrix protein PPIF (also called cyclophilin D). Importantly, inhibition of PPIF with NV556 significantly improved survival of mice with mitochondrial myopathy in which muscle mitochondria take up excessive amounts of Ca2+ also with intact ECM. In conclusion, skeletal muscle fibres isolated by collagenase-induced dissociation of the ECM display aberrant mitochondrial Ca2+ uptake, which involves a PPIF-dependent mitochondrial Ca2+ influx resembling that observed in mitochondrial myopathies.

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