Gent, Luke, Schwalbe, Ed and Procopio, Noemi (2023) The impact of maceration on the ‘Osteo-ome’; a pilot investigation. Journal of Proteomics, 271. p. 104754. ISSN 1874-3919
|
Text
1-s2.0-S1874391922002780-main.pdf - Published Version Available under License Creative Commons Attribution 4.0. Download (4MB) | Preview |
Abstract
The bone proteome, i.e., the ‘osteo-ome’, is a rich source of information for forensic studies. There have been advances in the study of biomolecule biomarkers for age-at-death (AAD) and post-mortem interval (PMI) estimations, by looking at changes in protein abundance and post-translational modifications (PTMs) at the peptide level. However, the extent to which other post-mortem factors alter the proteome, including ‘maceration’ procedures adopted in human taphonomy facilities (HTFs) to clean bones for osteological collections, is poorly understood. This pilot study aimed to characterise the impact of these ‘cleaning’ methods for de-fleshing skeletons on bone biomolecules, and therefore, what further impact this may have on putative biomarkers in future investigations. Three specific maceration procedures, varying in submersion time (one week or two days) and water temperature (55 °C or 87 °C) were conducted on six bovid tibiae from three individual bovines; the proteome of fresh and macerated bones of each individual was compared. The maceration at 87 °C for two days had the greatest proteomic impact, decreasing protein relative abundances and inducing specific PTMs. Overall, these results suggest that routinely-employed maceration procedures are harsh, variable and potentially threaten the viability of discovering new forensic biomarkers in macerated skeletal remains.
Item Type: | Article |
---|---|
Additional Information: | Funding information: The authors acknowledge the UKRI for supporting this work by a UKRI Future Leaders Fellowship (N.P.) under grant MR/S032878/1. We also acknowledge the technical support of The Newcastle University Protein and Proteome Analysis (NUPPA) core facility for mass spectrometry analyses. The graphical abstract was created with BioRender.com. |
Subjects: | C700 Molecular Biology, Biophysics and Biochemistry |
Department: | Faculties > Health and Life Sciences > Applied Sciences |
Depositing User: | Elena Carlaw |
Date Deposited: | 04 Nov 2022 15:58 |
Last Modified: | 04 Nov 2022 16:00 |
URI: | https://nrl.northumbria.ac.uk/id/eprint/50550 |
Downloads
Downloads per month over past year