Spatial analysis of the ancient proteome of archeological teeth using mass spectrometry imaging.

Spatial analysis of the ancient proteome of archeological teeth using mass spectrometry imaging.
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使用质谱成像对考古牙齿的古代蛋白质组进行空间分析。

DOI:
10.1002/rcm.9486
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发表时间:
2023
期刊:
RCM
影响因子:
--
通讯作者:
Dekker J
Dekker J
中科院分区:
--
文献类型:
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作者:
Dekker J

文献摘要

相似文献

从考古骨骼和牙齿中提取的蛋白质用于研究灭绝和现存物种的生殖发育,过去个体的生物性别和年龄,以及古代健康和生理学。然而,可变的蛋白质保存在考古materials.MethodsTo更好地了解牙齿内保存的古代蛋白质的空间分布,我们应用基质辅助激光解吸/电离质谱成像(MALDI-MSI)的第一次生物考古样品可视化的强度考古牙齿薄切片的蛋白质。我们专门探讨了四种蛋白质的空间分布(I型胶原蛋白,其中链α-1和α-2,α-2-HS-糖蛋白,血红蛋白亚基α和肌球蛋白轻多肽6)。数据可通过ProteomeXchange获得,标识符为PXD 038114。然而,我们观察到,肽并不总是遵循我们的假设,他们的空间分布,观察到几种蛋白质的空间分布有明显的差异,偶尔在同一蛋白质的肽之间。我们已经证明,MALDI-MSI可以成功地应用于矿化的生物考古组织,以检测古老的肽。在未来的应用中,这项技术可能特别富有成效,不仅可以了解一系列考古材料中蛋白质的保存情况,还可以就采样策略和考古和生物学意义的关键蛋白质的目标做出明智的决定。
RationaleProteins extracted from archaeological bone and teeth are utilised for investigating the phylogeny of extinct and extant species, the biological sex and age of past individuals, as well as ancient health and physiology. However, variable preservation of proteins in archaeological materials represents a major challenge.MethodsTo better understand the spatial distribution of ancient proteins preserved within teeth, we applied matrix assisted laser desorption/ionisation mass spectrometry imaging (MALDI‐MSI) for the first time to bioarchaeological samples to visualise the intensity of proteins in archaeological teeth thin sections. We specifically explored the spatial distribution of four proteins (collagen type I, of which the chains alpha‐1 and alpha‐2, alpha‐2‐HS‐glycoprotein, haemoglobin subunit alpha and myosin light polypeptide 6).ResultsWe successfully identified ancient proteins in archaeological teeth thin sections using mass spectrometry imaging. The data are available via ProteomeXchange with identifier PXD038114. However, we observed that peptides did not always follow our hypotheses for their spatial distribution, with distinct differences observed in the spatial distribution of several proteins, and occasionally between peptides of the same protein.ConclusionsWhile it remains unclear what causes these differences in protein intensity distribution within teeth, as revealed by MALDI‐MSI in this study, we have demonstrated that MALDI‐MSI can be successfully applied to mineralised bioarchaeological tissues to detect ancient peptides. In future applications, this technique could be particularly fruitful not just for understanding the preservation of proteins in a range of archaeological materials, but making informed decisions on sampling strategies and the targeting of key proteins of archaeological and biological interest.