{"id":{"repo_id":"brock","oai_identifier":"oai:brocku.scholaris.ca:10464/4195"},"canonical_url":"https://search.dev.ndltd.org/etd/brock/oai:brocku.scholaris.ca:10464/4195","repository":{"repo_id":"brock","name":"Brock University","base_url":"https://brocku.scholaris.ca/server/oai/request"},"display":{"title":"Regulation of Protein Turnover during Hyper-osmotic Stress in Skeletal Muscle","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Vandommele, Cody"],"institution":"Brock University","degree_name":"M.Sc. Applied Health Sciences","degree_level":"Masters","degree_discipline":"Faculty of Applied Health Sciences","degree_department":"Applied Health Sciences Program","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-02-12","date_published":"2013-02-12","updated_at":"2026-07-24T01:23:02Z","subjects":["osmotic","stress","skeletal muscle","protein turnover"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10464/4195","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Applied Health Sciences Program"]},{"key":"dc:creator","label":"Author","values":["Vandommele, Cody"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2013-02-12T15:49:38Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2013-02-12T15:49:38Z"]},{"key":"dc:date.issued","label":"Date","values":["2013-02-12"]},{"key":"dc:type","label":"Dc Type","values":["Electronic Thesis or Dissertation"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Faculty of Applied Health Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.Sc. 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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."]},{"key":"dc:title","label":"Title","values":["Regulation of Protein Turnover during Hyper-osmotic Stress in Skeletal Muscle"]}]}],"canonical_facts":{"dc:contributor.department":["Applied Health Sciences Program"],"dc:creator":["Vandommele, Cody"],"dc:date.accessioned":["2013-02-12T15:49:38Z"],"dc:date.available":["2013-02-12T15:49:38Z"],"dc:date.issued":["2013-02-12"],"dc:description.abstract":["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."],"dc:identifier.uri":["http://hdl.handle.net/10464/4195"],"dc:language.iso":["eng"],"dc:subject":["osmotic","stress","skeletal muscle","protein turnover"],"dc:title":["Regulation of Protein Turnover during Hyper-osmotic Stress in Skeletal Muscle"],"dc:type":["Electronic Thesis or Dissertation"],"thesis:degree_discipline":["Faculty of Applied Health Sciences"],"thesis:degree_level":["Masters"],"thesis:degree_name":["M.Sc. Applied Health Sciences"],"thesis:institution_name":["Brock University"]},"updated_at":"2026-07-24T01:23:02Z"}