Mass spectrometry proteomic profiling of postmortem human muscle degradation for PMI estimation

IF 2.5 3区医学 Q1 MEDICINE, LEGAL Forensic science international Pub Date : 2024-12-01 Epub Date: 2024-10-20 DOI:10.1016/j.forsciint.2024.112256

Paolo Bailo , Daniele Capitanio , Alessio Battistini , Danilo De Angelis , Manuela Moriggi , Stefano Tambuzzi , Matteo Marchesi , Sergio Vedovati , Marco Enrico Giovanni Arosio , Francesco Auxilia , Cecilia Gelfi , Andrea Piccinini

{"title":"Mass spectrometry proteomic profiling of postmortem human muscle degradation for PMI estimation","authors":"Paolo Bailo , Daniele Capitanio , Alessio Battistini , Danilo De Angelis , Manuela Moriggi , Stefano Tambuzzi , Matteo Marchesi , Sergio Vedovati , Marco Enrico Giovanni Arosio , Francesco Auxilia , Cecilia Gelfi , Andrea Piccinini","doi":"10.1016/j.forsciint.2024.112256","DOIUrl":null,"url":null,"abstract":"<div><div>The discovery of new methods for determining the post-mortem interval is of significant forensic interest. Mass spectrometry has enhanced the accuracy of assessing post-mortem protein decay, with skeletal muscle being the most studied substrate due to its intrinsic properties of postmortem decay. In this pilot study, human skeletal muscle tissue (iliopsoas) was harvested and allowed to decay under controlled temperature and humidity conditions at predetermined intervals.</div><div>The samples were analyzed using mass spectrometry proteomics for both qualitative and quantitative evaluation of proteins and peptides. Candidate proteins were validated through immunoblotting.</div><div>The results were significant, identifying several proteins that could aid in estimating the post-mortem interval. Notably, PLIN4, MYOZ2, SYNPO2, and BAG3 were validated by immunoblotting over a broader range of experimental points and temperatures. Furthermore, human results were compared with animal muscle samples from a previous study, revealing similarities in decomposition kinetics.</div><div>This analysis of human samples marks a step forward in the potential forensic application of proteomic evaluation by mass spectrometry.</div></div>","PeriodicalId":12341,"journal":{"name":"Forensic science international","volume":"365 ","pages":"Article 112256"},"PeriodicalIF":2.5000,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Forensic science international","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0379073824003384","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/10/20 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"MEDICINE, LEGAL","Score":null,"Total":0}

引用次数: 0

Abstract

The discovery of new methods for determining the post-mortem interval is of significant forensic interest. Mass spectrometry has enhanced the accuracy of assessing post-mortem protein decay, with skeletal muscle being the most studied substrate due to its intrinsic properties of postmortem decay. In this pilot study, human skeletal muscle tissue (iliopsoas) was harvested and allowed to decay under controlled temperature and humidity conditions at predetermined intervals.

The samples were analyzed using mass spectrometry proteomics for both qualitative and quantitative evaluation of proteins and peptides. Candidate proteins were validated through immunoblotting.

The results were significant, identifying several proteins that could aid in estimating the post-mortem interval. Notably, PLIN4, MYOZ2, SYNPO2, and BAG3 were validated by immunoblotting over a broader range of experimental points and temperatures. Furthermore, human results were compared with animal muscle samples from a previous study, revealing similarities in decomposition kinetics.

This analysis of human samples marks a step forward in the potential forensic application of proteomic evaluation by mass spectrometry.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

质谱分析人类死后肌肉降解的蛋白质组谱，以估算 PMI。

发现确定死后间隔时间的新方法具有重要的法医学意义。质谱法提高了评估死后蛋白质衰变的准确性，而骨骼肌因其死后衰变的固有特性成为研究最多的基质。在这项试验性研究中，我们采集了人体骨骼肌组织（髂腰肌），并让其在受控的温度和湿度条件下按预定时间间隔衰变。样本采用质谱蛋白质组学进行分析，对蛋白质和肽进行定性和定量评估。候选蛋白质通过免疫印迹进行验证。结果非常显著，确定了几种有助于估计死后间隔的蛋白质。值得注意的是，PLIN4、MYOZ2、SYNPO2 和 BAG3 通过免疫印迹法在更广泛的实验点和温度范围内得到了验证。此外，还将人体结果与之前研究中的动物肌肉样本进行了比较，发现两者在分解动力学方面有相似之处。对人体样本的分析标志着质谱法蛋白质组评估在潜在法医应用方面向前迈进了一步。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Forensic science international 医学-医学：法

CiteScore

5.00

自引率

9.10%

发文量

285

审稿时长

49 days

期刊介绍： Forensic Science International is the flagship journal in the prestigious Forensic Science International family, publishing the most innovative, cutting-edge, and influential contributions across the forensic sciences. Fields include: forensic pathology and histochemistry, chemistry, biochemistry and toxicology, biology, serology, odontology, psychiatry, anthropology, digital forensics, the physical sciences, firearms, and document examination, as well as investigations of value to public health in its broadest sense, and the important marginal area where science and medicine interact with the law. The journal publishes: Case Reports Commentaries Letters to the Editor Original Research Papers (Regular Papers) Rapid Communications Review Articles Technical Notes.