scholarly journals PlanHab (Planetary Habitat Simulation): the combined and separate effects of 21 days bed rest and hypoxic confinement on human skeletal muscle miRNA expression

2016 ◽  
Vol 4 (8) ◽  
pp. e12753 ◽  
Author(s):  
Eric Rullman ◽  
Igor B. Mekjavic ◽  
Helene Fischer ◽  
Ola Eiken
2006 ◽  
Vol 97 (3) ◽  
pp. 261-271 ◽  
Author(s):  
Dieter Blottner ◽  
Michele Salanova ◽  
Britta Püttmann ◽  
Gudrun Schiffl ◽  
Dieter Felsenberg ◽  
...  

2014 ◽  
Vol 210 (3) ◽  
pp. 655-666 ◽  
Author(s):  
T. Režen ◽  
A. Kovanda ◽  
O. Eiken ◽  
I. B. Mekjavic ◽  
B. Rogelj

2018 ◽  
Vol 50 (9) ◽  
pp. 746-757 ◽  
Author(s):  
Yoshitake Cho ◽  
Robert S. Ross

Immobilization, bed rest, or denervation leads to muscle disuse and subsequent skeletal muscle atrophy. Muscle atrophy can also occur as a component of various chronic diseases such as cancer, AIDS, sepsis, diabetes, and chronic heart failure or as a direct result of genetic muscle disorders. In addition to this atrophic loss of muscle mass, metabolic deregulation of muscle also occurs. In contrast, physical exercise plays a beneficial role in counteracting disuse-induced atrophy by increasing muscle mass and strength. Along with this, exercise can also reduce mitochondrial dysfunction and metabolic deregulation. Still, while exercise causes valuable metabolic and functional adaptations in skeletal muscle, the mechanisms and effectors that lead to these changes such as increased mitochondria content or enhanced protein synthesis are not fully understood. Therefore, mechanistic insights may ultimately provide novel ways to treat disuse induced atrophy and metabolic deregulation. Mass spectrometry (MS)-based proteomics offers enormous promise for investigating the molecular mechanisms underlying disuse and exercise-induced changes in skeletal muscle. This review will focus on initial findings uncovered by using proteomics approaches with human skeletal muscle specimens and discuss their potential for the future study.


2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Michele Salanova ◽  
Gudrun Schiffl ◽  
Martina Gutsmann ◽  
Dieter Felsenberg ◽  
Daniel Belavý ◽  
...  

2004 ◽  
Vol 18 (11) ◽  
pp. 1228-1230 ◽  
Author(s):  
Jana Rudnick ◽  
Britta Püttmann ◽  
Per A. Tesch ◽  
Björn Alkner ◽  
Benedikt G. H. Schoser ◽  
...  

1999 ◽  
Vol 86 (2) ◽  
pp. 455-460 ◽  
Author(s):  
J. L. Andersen ◽  
T. Gruschy-Knudsen ◽  
C. Sandri ◽  
L. Larsson ◽  
S. Schiaffino

The effects of a 37-day period of bed rest on myosin heavy chain (MHC) expression on both mRNA and protein level in human skeletal muscle fibers were studied. Muscle biopsies from vastus lateralis muscle were obtained from seven healthy young male subjects before and after the bed-rest period. Combined in situ hybridization, immunocytochemistry, and ATPase histochemistry analysis of serial sections of the muscle biopsies demonstrated that fibers showing a mismatch between MHC isoforms at the mRNA and protein level increased significantly after the bed-rest period, suggesting an increase in the amount of muscle fibers in a transitional state. Accordingly, fibers showing a match in expression of MHC-1 and of MHC-2A at the mRNA and protein level decreased, whereas fibers showing a match between MHC-2X mRNA and protein increased after bed rest. Overall, there was an increase in fibers in a transitional state from phenotypic type 1 → 2A and 2A → 2X. Furthermore, a number of fibers with unusual MHC mRNA and isoprotein combinations were observed after bed rest (e.g., type 1 fibers with only mRNA for 2X and type 1 fibers negative for mRNA for MHC-β/slow, 2A, and 2X). In contrast, no changes were revealed after an examination at the protein level alone. These data suggest that the reduced load-bearing activity imposed on the skeletal muscles through bed rest will alter MHC gene expression, resulting in combinations of mRNA and MHC isoforms normally not (or only rarely) observed in muscles subjected to load-bearing activity. On the other hand, the present data also show that 37 days of bed rest are not a sufficient stimulus to induce a similar change at the protein level, as was observed at the gene level.


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