Regulation of Protein Turnover during Hyper-osmotic Stress in Skeletal Muscle

The purpose of this study was to examine the effect of hyper-osmotic stress on protein turnover in skeletal muscle tissue using an established in-vitro model. Rat EDL muscles were incubated in either hyper-osmotic (400 ± 10 Osm) or isoosmotic (290 ± 10 Osm) custom-modified media (Gibco). L-[14C]-U-phenylalanine (n=8) and cycloheximide (n=8) were used to quantify protein synthesis and degradation, respectively. Western blotting analyses was performed to determine the activation of protein synthesis and degradation pathways. During hyperosmotic stress, protein degradation increased (p<0.05), while protein synthesis was decreased (p<0.05) as compared to the iso-osmotic condition. The decline in protein synthesis was accompanied by a decrease (p<0.05) in p70s6 kinase phosphorylation, while the increase in protein degradation was associated with an increase (p<0.05) in autolyzed calpain. Therefore, hyper-osmotic extracellular stress results in an intracellular catabolic environment in mammalian skeletal muscle tissue.

Name thesis:degree_name

M.Sc. Applied Health Sciences

Level thesis:degree_level

Masters

Discipline thesis:degree_discipline

Faculty of Applied Health Sciences

Department dc:contributor.department

Applied Health Sciences Program

Grantor

Brock University

Year dc:date.issued

2013

Author dc:creator

• Vandommele, Cody

• osmotic
• stress
• skeletal muscle
• protein turnover

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/10464/4195

OAI identifier oai:identifier

oai:brocku.scholaris.ca:10464/4195