ArticleJournal of the Royal Society, Interface2020
Protein aggregate formation permits millennium-old brain preservation.
Article in Journal of the Royal Society, Interface, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Molecular Solution to the Paradox of Ancient Brain Preservation.Journal of proteome research · 2026Article
- New approach to specific Alzheimer's disease diagnosis based on plasma biomarkers in a cognitive disorder cohort.European journal of clinical investigation · 2025Article
- Proteolysis-Based Biomarker Repertoire of the Neurofilament Proteome.Journal of neurochemistry · 2025Article
- Article
- A novel integrated extraction protocol for multi-omic studies in heavily degraded samples.Scientific reports · 2024Article
- Neurofilaments as biomarkers in neurological disorders - towards clinical application.Nature reviews. Neurology · 2024Review
- Human brains preserve in diverse environments for at least 12 000 years.Proceedings. Biological sciences · 2024Article
- Postmortem changes in brain cell structure: a review.Free neuropathology · 2023Article
- Article
- The 2022 Lady Estelle Wolfson lectureship on neurofilaments.Journal of neurochemistry · 2022Review
- Paleoproteomics.Chemical reviews · 2022Review
- Blood GFAP as an emerging biomarker in brain and spinal cord disorders.Nature reviews. Neurology · 2022Review
- Serum neurofilament light chain withstands delayed freezing and repeated thawing.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human proteins have not been reported to survive in free nature, at ambient temperature, for long periods. Particularly, the human brain rapidly dissolves after death due to auto-proteolysis and putrefaction. The here presented discovery of 2600-year-old brain proteins from a radiocarbon dated human brain provides new evidence for extraordinary long-term stability of non-amyloid protein aggregates. Immunoelectron microscopy confirmed the preservation of neurocytoarchitecture in the ancient brain, which appeared shrunken and compact compared to a modern brain. Resolution of intermediate filaments (IFs) from protein aggregates took 2-12 months. Immunoassays on micro-dissected brain tissue homogenates revealed the preservation of the known protein topography for grey and white matter for type III (glial fibrillary acidic protein, GFAP) and IV (neurofilaments, Nfs) IFs. Mass spectrometry data could be matched to a number of peptide sequences, notably for GFAP and Nfs. Preserved immunogenicity of the prehistoric human brain proteins was demonstrated by antibody generation (GFAP, Nfs, myelin basic protein). Unlike brain proteins, DNA was of poor quality preventing reliable sequencing. These long-term data from a unique ancient human brain demonstrate that aggregate formation permits for the preservation of brain proteins for millennia.
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Registered trials
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