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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.

Titel:	Protein aggregate formation permits millennium-old brain preservation.
Autor/in / Beteiligte Person:	Petzold, A ; Lu, CH ; Groves, M ; Gobom, J ; Zetterberg, H ; Shaw, G ; O'Connor, S
Link:	Full Text Finder (Volltext)
Zeitschrift:	Journal of the Royal Society, Interface, Jg. 17 (2020), Heft 162, S. 20190775
Veröffentlichung:	London : Royal Society, [2004]-, 2020
Medientyp:	academicJournal
ISSN:	1742-5662 (electronic)
DOI:	10.1098/rsif.2019.0775
Schlagwort:	Amino Acid Sequence Glial Fibrillary Acidic Protein metabolism Humans Brain metabolism Protein Aggregates
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [J R Soc Interface] 2020 Jan; Vol. 17 (162), pp. 20190775. <i>Date of Electronic Publication: </i>2020 Jan 08. MeSH Terms: Brain* / metabolism ; Protein Aggregates* ; Amino Acid Sequence ; Glial Fibrillary Acidic Protein / metabolism ; Humans References: Am J Psychiatry. 2014 Mar;171(3):265-74. (PMID: 24585329) ; J R Soc Interface. 2011 Aug 7;8(61):1104-13. (PMID: 21247950) ; Bioinformatics. 2017 Nov 1;33(21):3471-3472. (PMID: 28520855) ; Science. 1985 Jun 14;228(4705):1280-4. (PMID: 4001942) ; Science. 2012 Sep 21;337(6101):1460-1. (PMID: 22997313) ; J R Soc Interface. 2017 Apr;14(129):. (PMID: 28446704) ; Science. 1981 Sep 25;213(4515):1521-2. (PMID: 6169146) ; J Immunol Methods. 2003 Jul;278(1-2):179-90. (PMID: 12957406) ; Proc Biol Sci. 2017 May 31;284(1855):. (PMID: 28566488) ; J Biol Chem. 2016 Mar 25;291(13):6681-8. 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Protein aggregate formation permits millennium-old brain preservation.