Abstract

An accurate estimation of the postmortem interval (PMI) is a central aspect in forensic routine. Recently, a novel approach based on the analysis of postmortem muscle protein degradation has been proposed. However, a number of questions remain to be answered until sensible application of this method to a broad variety of forensic cases is possible. To evaluate whether altered in vivo protein metabolism interferes with postmortem degradation patterns, we conducted a comparative study. We developed a standardized animal degradation model in rats, and collected additional muscle samples from animals recovering from muscle injury and from rats with developed disuse muscle atrophy after induced spinal cord injury. All samples were analyzed by SDS-PAGE and Western blot, labeling well-characterized muscle proteins. Tropomyosin was found to be stable throughout the investigated PMI and no alterations were detected in regenerating and atrophic muscles. In contrast, significant predictable postmortem changes occurred in desmin and vinculin protein band patterns. While no significant deviations from native patterns were detected in at-death samples of disuse muscle atrophy, interestingly, samples of rats recovering from muscle injury revealed additional desmin and vinculin degradation bands that did not occur in this form in any of the examined postmortem samples regardless of PMI. It remains to be investigated whether in vivo-altered metabolism influences postmortem degradation kinetics or if such muscle samples undergo postmortem degradation in a regular fashion.

Highlights

  • To figure out when a person died can have major implications in ongoing criminal investigations but can play a role in inheritance law and other legal issues

  • We found indication for no major interference of enhanced antemortem protein turnover in Bzero-hour samples,^ it is implied to investigate whether there could be influence on postmortem degradation kinetics

  • In cases of muscle regeneration with necrotic tissue, in which there is a deviation of band appearance compared to healthy tissue, it seems worth to further test whether the investigated proteins undergo postmortem degradation in a regular fashion, or whether kinetics are altered

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Summary

Introduction

To figure out when a person died can have major implications in ongoing criminal investigations but can play a role in inheritance law and other legal issues. The most commonly used methods to date include the measurement and comparison of body and environmental temperature [1], the examination of so called supravital reactions [2], the. Among those questions is the demand of discriminability of postmortem protein degradation patterns from those of altered in vivo protein metabolism. As the 26S proteasome [12], the autophagy-lysosomal pathway [13], and the catalytic activation of caspases [14] require ATP, which is depleted in postmortem conditions [15], the Ca2+-activated calpains are considered to predominately contribute in postmortem stages [16, 17]. Postmortem decomposition of skeletal muscle by the calpain system has been described in detail by studies in context of increasing meat tenderness upon storage time and conditions [16]

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