title: Skeletal muscle proteins: a new approach to delimitate the time since death.
abstract: OBJECTIVE
  Skeletal muscle tissue is proposed as a forensic model tissue with strong potential, as it is easily accessible and its true-to-life state structure and function is well known. Despite this strong potential, skeletal muscle degradation studies are rare. The aim of this study was to test if a skeletal muscle-based protein analysis is applicable to delimitate the time since death.
  
  
  METHODS
  Under standard conditions, two pigs were stored either at 22 °C for 5 days or 4 °C for 21 days. Their Mm. biceps femori were sampled periodically for analyses of ten skeletal muscle proteins postmortem.
  
  
  RESULTS
  All analyzed proteins can serve as markers for a delimitation of the time since death. Desmin, nebulin, titin, and SERCA 1 displayed distinct protein patterns at certain points of time. The other five proteins, α-actinin, calsequestrin-1, laminin, troponin T-C, and SERCA 2, showed no degradation patterns within the analyzed postmortem time frame.
  
  
  CONCLUSIONS
  Referring to specific skeletal muscle proteins, results showed short-term stabilities for just a minority of analyzed proteins, while the majority of investigated proteins displayed characteristics as long-term markers. Due to specific patterns and the possibility to determine definite constraints of the presence, absence, or pattern alterations of single proteins, the feasibility of porcine skeletal muscle as forensic model tissue is outlined and the potential of skeletal muscle as forensic model tissue is underlined, especially with respect to later postmortem phases, which so far lack feasible methods to delimitate the time since death.
authors.affiliation: University of Salzburg, Salzburg, Austria. esra.foditsch@gmail.com.
authors.forename: Elena Esra
authors.initials: EE
authors.lastname: Foditsch
authors.affiliation: University of Salzburg, Salzburg, Austria.
authors.forename: Alexandra Maria
authors.initials: AM
authors.lastname: Saenger
authors.affiliation: University of Salzburg, Salzburg, Austria.
authors.forename: Fabio Carlo
authors.initials: FC
authors.lastname: Monticelli
mesh_terms: D000185:Actinin / Q000378:metabolism; D000818:Animals; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000378:metabolism; D002155:Calsequestrin; D064211:Connectin / Q000378:metabolism; D003893:Desmin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D049429:Forensic Pathology; D007797:Laminin / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000378:metabolism; D023421:Models, Animal; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D011180:Postmortem Changes; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000378:metabolism; D013552:Swine; D019209:Troponin C / Q000378:metabolism; D020107:Troponin T / Q000378:metabolism
chemical_list: C503129:CASQ1 protein, human; D002135:Calcium-Binding Proteins; D002155:Calsequestrin; D064211:Connectin; D003893:Desmin; D007797:Laminin; D024101:Mitochondrial Proteins; D009124:Muscle Proteins; D019209:Troponin C; D020107:Troponin T; C035620:nebulin; D000185:Actinin; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases; C506943:ATP2A1 protein, human; C506946:ATP2A2 protein, human
keywords: Post mortem; Proteins; Skeletal muscle; Time of death; Western blot