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Effects of postmortem delays on protein composition and oxidation
Zeinab ElHajj1, Amélie Cachot1, Terry Müller1
1Proteomic Unit, Centre for Psychiatric Neuroscience, Department of Psychiatry, CHUV, CERY, CH-1008 Lausanne, Switzerland.
Brain Research Bulletin
|January 22, 2016
Summary
Postmortem interval affects protein integrity in mouse brains, with significant degradation observed after 6 hours. Modifications like S-nitrosylation and carbonylation varied, highlighting the need to consider postmortem delay in neurodegenerative disease research.
Area of Science:
- Neuroscience
- Biochemistry
- Proteomics
Background:
- Human autopsy brain tissue is crucial for studying neurodegenerative diseases like Alzheimer's and Parkinson's.
- Evaluating postmortem effects on protein composition, modification, and degradation is essential for accurate data interpretation.
- Postmortem delays can significantly alter the molecular landscape of brain tissue.
Purpose of the Study:
- To investigate the impact of varying postmortem delays (0h, 6h, 24h) on protein composition, proteolysis, and posttranslational modifications in mouse brain tissue.
- To assess changes in proteins relevant to Alzheimer's disease (AD), including cytoskeletal, synaptic, and inflammatory proteins.
- To specifically examine alterations in S-nitrosylation, carbonylation, and ubiquitination.
Main Methods:
- Analysis of mouse brain tissues subjected to postmortem delays of 0, 6, and 24 hours.
- Proteomic analysis to evaluate changes in protein composition and degradation.
- Assessment of specific posttranslational modifications: S-nitrosylation, carbonylation, and ubiquitination.
Main Results:
- Several proteins exhibited resistance to degradation within the first 6 hours postmortem, with degradation commencing thereafter.
- S-nitrosylation and carbonylation levels remained relatively stable, except in proteins susceptible to degradation.
- Brain spectrin showed S-nitrosylation at death, with S-nitrosylated degradation fragments detected at 24 hours postmortem.
- Ubiquitination and carbonylation were minimally affected within the first 24 hours postmortem.
Conclusions:
- Postmortem interval significantly influences protein integrity and modification in brain tissue.
- Certain proteins are more vulnerable to degradation than others over time.
- The findings underscore the importance of accounting for postmortem delay when analyzing human brain tissue for neurodegenerative disease research.
- The physiological role and dynamic changes of S-nitrosylation require further investigation.
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