Archaeological collagen: Why worry about collagen diagenesis?

Dobberstein, Reimer C.; Collins, Matthew J.; Craig, Oliver E.; Taylor, Gillian; Penkman, Kirsty; Ritz‐Timme, Stefanie

doi:10.1007/s12520-009-0002-7

Cited by 128 publications

(102 citation statements)

References 54 publications

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“…Even this technique's strongest proponents acknowledge, however, that AAA will also fail to identify all cases of contamination, that serious methodological issues exist with such analysis (Harbeck and Grupe, 2009:55;Hedges and van Klinken, 1992; van Klinken, 1999), and that the amino acid composition of collagen extracts does not vary significantly until collagen is almost entirely degraded (Beeley and Lunt, 1980;Dobberstein et al, 2009;van Klinken, 1999). Furthermore, given the cost of such analysis (US$100e200 per sample), and as van Klinken (1999:690) found specific amino acid assays to be "relatively unhelpful for the assessment of 'collagen' quality," above and beyond those identified by chemical and elemental measures, we chose not to attempt to assess the preservation of these samples by AAA.…”

Section: Methodsmentioning

confidence: 99%

Bone collagen preservation in the tropics: a case study from ancient Puerto Rico

Pestle

Colvard

2012

Journal of Archaeological Science

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Section: Methodsmentioning

confidence: 99%

Bone collagen preservation in the tropics: a case study from ancient Puerto Rico

Pestle

Colvard

2012

Journal of Archaeological Science

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“…As such, additional controlled studies on the influence of various diagenetic processes (e.g. Dobberstein et al, 2008Dobberstein et al, , 2009Harbeck and Grupe, 2009) on the bones of mammals, fish and birds would be extremely beneficial.…”

Section: Bonementioning

confidence: 99%

“…To date, a number of studies have attempted to define and refine such criteria (Ambrose, 1990;DeNiro, 1985;DeNiro and Weiner, 1988;Dobberstein et al, 2009;Grupe and Turban-Just, 1998;Grupe et al, 2000;Harbeck and Grupe, 2009;Schoeninger et al, 1989;Tuross et al, 1988Tuross et al, , 1989van Klinken, 1999), but all have focused exclusively on mammalian bone. One notable exception is the work of Nehlich and Richards (2009), who suggested that because of differences in the amino acid composition of collagen, the quality criteria for sulfur isotopic analysis (C:S ratio) should be different for fish and mammalian bone.…”

Section: Introductionmentioning

confidence: 99%

Fish bone chemistry and ultrastructure: implications for taphonomy and stable isotope analysis

Szpak

2011

Journal of Archaeological Science

246

172

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“…In addition, the rate of these degradation pathways are affected by temperature, as higher burial temperatures have been shown to accelerate these processes (6,8). Though relatively unusual, the first of these three pathways results in a slower deterioration process, which is more generally mitigated under (6) specific environmental constraints, such as geochemical stability (stable temperature and acidity) that promote bone mineral preservation.…”

mentioning

confidence: 99%

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen

Hill

Wither

Nemkov

et al. 2015

Molecular & Cellular Proteomics

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Bone samples from several vertebrates were collected from the Ziegler Reservoir fossil site, in Snowmass Village, Colorado, and processed for proteomics analysis. The specimens come from Pleistocene megafauna Bison latifrons, dating back ϳ120,000 years. Proteomics analysis using a simplified sample preparation procedure and tandem mass spectrometry (MS/MS) was applied to obtain protein identifications. Several bioinformatics resources were used to obtain peptide identifications based on sequence homology to extant species with annotated genomes. With the exception of soil sample controls, all samples resulted in confident peptide identifications that mapped to type I collagen. In addition, we analyzed a specimen from the extinct B. latifrons that yielded peptide identifications mapping to over 33 bovine proteins. Our analysis resulted in extensive fibrillar collagen sequence coverage, including the identification of posttranslational modifications. Hydroxylysine glucosylgalactosylation, a modification thought to be involved in collagen fiber formation and bone mineralization, was identified for the first time in an ancient protein dataset. Meta-analysis of data from other studies indicates that this modification may be common in well-preserved prehistoric samples. Additional peptide sequences from extracellular matrix (ECM) and non-ECM proteins have also been identified for the first time in ancient tissue samples. These data provide a framework for analyzing ancient protein signatures in wellpreserved fossil specimens, while also contributing novel insights into the molecular basis of organic matter preservation. As such, this analysis has unearthed common posttranslational modifications of collagen that may assist in its preservation over time. During the last decade, paleontology and taphonomy (the study of decaying organisms over time and the fossilization processes) have begun to overlap with the field of proteomics to shed new light on preserved organic matter in fossilized bones (1-4). These bones represent a time capsule of ancient biomolecules, owing to their natural resistance to post mortem decay arising from a unique combination of mechanical, structural, and chemical properties (4 -7).Although bones can be cursorily described as a composite of collagen (protein) and hydroxyapatite (mineral), fossilized bones undergo three distinct diagenesis pathways: (i) chemical deterioration of the organic phase; (ii) chemical deterioration of the mineral phase; and (iii) (micro)biological attack of the composite (6). In addition, the rate of these degradation pathways are affected by temperature, as higher burial temperatures have been shown to accelerate these processes (6,8). Though relatively unusual, the first of these three pathways results in a slower deterioration process, which is more generally mitigated under (6) specific environmental constraints, such as geochemical stability (stable temperature and acidity) that promote bone mineral preservation. Importantly, slower deterioration results in more pre...

show abstract

Archaeological collagen: Why worry about collagen diagenesis?

Abstract: DNA appears to decay by random chain scission resulting in a predictable range of fragment lengths.

Cited by 128 publications

References 54 publications

Bone collagen preservation in the tropics: a case study from ancient Puerto Rico

Bone collagen preservation in the tropics: a case study from ancient Puerto Rico

Fish bone chemistry and ultrastructure: implications for taphonomy and stable isotope analysis

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen

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