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Protein aggregate formation permits millennium-old brain preservation

Journal article
Authors A. Petzold
C. H. Lu
M. Groves
Johan Gobom
Henrik Zetterberg
G. Shaw
S. O'Connor
Published in Journal of the Royal Society Interface
Volume 17
Issue 162
ISSN 1742-5689
Publication year 2020
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Language en
Links dx.doi.org/10.1098/rsif.2019.0775
Keywords biomarker, neurofilament, glial fibrillary acidic protein, protein, aggregation, neurodegeneration, archaeology, multiple-sclerosis, neurofilament proteins, alzheimers-disease, nf-h, phosphorylation, biomarker, markers, elisa, transmission, instability, Science & Technology - Other Topics
Subject categories Neurosciences

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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