Activity, abundance and expression of Ca2+-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata

Verfasser / Beitragende:
[Beau Reilly, Rebecca Cramp, Craig Franklin]
Ort, Verlag, Jahr:
2015
Enthalten in:
Journal of Comparative Physiology B, 185/2(2015-02-01), 243-255
Format:
Artikel (online)
ID: 605514526
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024 7 0 |a 10.1007/s00360-014-0880-6  |2 doi 
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245 0 0 |a Activity, abundance and expression of Ca2+-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata  |h [Elektronische Daten]  |c [Beau Reilly, Rebecca Cramp, Craig Franklin] 
520 3 |a In most mammals, prolonged muscle disuse (e.g. bed-rest, limb casting or spaceflight) results in atrophy of muscle fibres which is largely due to unregulated proteolysis. Although numerous proteolytic pathways are known to participate in muscle disuse atrophy, recent evidence suggests that activation of Ca2+-dependent cysteine proteases (calpains) is required for disuse atrophy in limb skeletal muscles. In contrast to typical models of muscle disuse (humans and rodents), animals that experience natural bouts of chronic muscle inactivity, such as hibernating mammals and aestivating frogs, consistently exhibit limited or no change in skeletal muscle size. In the current study, we examined enzyme activity, protein abundance and gene expression levels of calpain isoforms in gastrocnemius muscle of the aestivating frog, Cyclorana alboguttata. We predicted that in aestivating C. alboguttata there would be a downregulation of the abundance, activity and gene expression of calpain 1 and calpain 2. In contrast to our hypothesis, there was no significant decrease in the enzyme activity levels or the relative protein abundances of calpain 1 and calpain 2. Similarly, gene expression assays (both qRT-PCR and RNA Seq data) indicated that calpains were unaffected by aestivation. Western blotting of ‘muscle-specific' calpain 3, which is consistently downregulated during atrophic conditions, indicated that this isoform is present in C. alboguttata muscle where it appears to be in its autolysed state. The absence of any increase in enzyme activity, protein and mRNA abundance of calpains in aestivators is consistent with the protection of gastrocnemius muscle against uncontrolled proteolysis throughout aestivation. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a Calpain  |2 nationallicence 
690 7 |a Proteolysis  |2 nationallicence 
690 7 |a Atrophy  |2 nationallicence 
690 7 |a Aestivation  |2 nationallicence 
690 7 |a Calcium  |2 nationallicence 
700 1 |a Reilly  |D Beau  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
700 1 |a Cramp  |D Rebecca  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
700 1 |a Franklin  |D Craig  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
773 0 |t Journal of Comparative Physiology B  |d Springer Berlin Heidelberg  |g 185/2(2015-02-01), 243-255  |x 0174-1578  |q 185:2<243  |1 2015  |2 185  |o 360 
856 4 0 |u https://doi.org/10.1007/s00360-014-0880-6  |q text/html  |z Onlinezugriff via DOI 
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900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
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950 |B NATIONALLICENCE  |P 700  |E 1-  |a Reilly  |D Beau  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cramp  |D Rebecca  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Franklin  |D Craig  |u School of Biological Sciences, The University of Queensland, 4072, Brisbane, QLD, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Journal of Comparative Physiology B  |d Springer Berlin Heidelberg  |g 185/2(2015-02-01), 243-255  |x 0174-1578  |q 185:2<243  |1 2015  |2 185  |o 360