Abstract
Estimating the time since death is a very important aspect in forensic sciences which is pursued by a variety of methods. The most precise method to determine the postmortem interval (PMI) is the temperature method which is based on the decrease of the body core temperature from 37 °C. However, this method is only useful in the early postmortem phase (~0–36 h). The aim of the present work is to develop an accurate method for PMI determination beyond this present limit. For this purpose, we used sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting, and casein zymography to analyze the time course of degradation of selected proteins and calpain activity in porcine biceps femoris muscle until 240 h postmortem (hpm). Our results demonstrate that titin, nebulin, desmin, cardiac troponin T, and SERCA1 degraded in a regular and predictable fashion in all samples investigated. Similarly, both the native calpain 1 and calpain 2 bands disintegrate into two bands subsequently. This degradation behavior identifies muscular proteins and enzymes as promising substrates for future molecular-based PMI determination technologies.
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Acknowledgments
The authors are grateful to Fiona Bergmann, Magdalena Brandauer, and Christian Platzl for providing excellent technical assistance, as well as Roman Fuchs and Arne Bathke for advices and assistance in statistics. Our gratitude also goes to Elena Esra Foditsch and Edith Tutsch-Bauer for exchange of ideas and discussion throughout the study.
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All applicable international, national, and/or institutional guidelines for the care and use of animals were followed.
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Pittner, S., Monticelli, F.C., Pfisterer, A. et al. Postmortem degradation of skeletal muscle proteins: a novel approach to determine the time since death. Int J Legal Med 130, 421–431 (2016). https://doi.org/10.1007/s00414-015-1210-6
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DOI: https://doi.org/10.1007/s00414-015-1210-6