title: Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress.
abstract: Acute heat stress negatively impacts both human health and livestock production. In order to characterize the skeletal muscle cellular response to acute heat stress, the muscle sarcoplasmic proteome was analyzed via 2-D DIGE. Pigs (n=8 per treatment) were exposed to one of the three treatments for 12 h: heat stress (HS; 37 °C), thermal neutral (TN; 21°C), or TN while pair-fed (PFTN; 21 °C, feed limited based on HS group consumption). After euthanasia, the semitendinosus muscle was excised, separated into predominately red (RST) and white (WST) fiber type portions, and sarcoplasmic proteins were extracted. Spots determined in 2D-DIGE to be different due to HS were identified using ESI-MS or LC-MS/MS. Several proteins involved in glycolysis, glycogenesis, and glycogenolysis were increased or modified, indicating enhanced glycolytic capacity in response to HS. In the WST, HS decreased abundance of tubulins and soluble actin and increased phosphorylated cofilin 2 abundance, indicating a loss of microtubule structure and a likely increase in stable actin microfilaments. HS increased manganese superoxide dismutase abundance, but decreased peroxiredoxin 2 abundance, indicating an antioxidant response to HS. The proteomic response to HS suggests marked cellular changes in carbohydrate metabolism, structure, and antioxidant machinery in skeletal muscle.
  
  
  CONCLUSIONS
  This paper examines the proteome response of skeletal muscle to acute (short duration, high intensity) heat stress (HS). Defining changes in the sarcoplasm proteome increases our understanding of the mechanisms of how muscle responds to HS. Moreover, demonstration of a fiber type differential response to HS illustrates the dynamic nature of muscle. The experimental design of the experiment allows for the differentiation between the true effects of HS and HS-induced hypophagia. Data such as these will provide the foundation for developing future mitigating solutions and preventative therapies to reduce the detrimental effects of acute heat stress on muscle function and metabolism.
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States. Electronic address: scruzen@iastate.edu.
authors.forename: S M
authors.initials: SM
authors.lastname: Cruzen
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
authors.forename: S C
authors.initials: SC
authors.lastname: Pearce
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
authors.forename: L H
authors.initials: LH
authors.lastname: Baumgard
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
authors.forename: N K
authors.initials: NK
authors.lastname: Gabler
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
authors.forename: E
authors.initials: E
authors.lastname: Huff-Lonergan
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
authors.forename: S M
authors.initials: SM
authors.lastname: Lonergan
mesh_terms: D000818:Animals; D020869:Gene Expression Profiling / Q000379:methods; D018869:Heat-Shock Response / Q000502:physiology*; D018656:Muscle Fibers, Fast-Twitch / Q000378:metabolism*; D018657:Muscle Fibers, Slow-Twitch / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism*; D020543:Proteome / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013552:Swine
chemical_list: D009124:Muscle Proteins; D020543:Proteome
keywords: Cytoskeleton; Heat shock proteins; Heat stress; Metabolism; Pigs; Skeletal muscle