New strategies for characterizing ancient proteins using matrix-assisted laser desorption ionization mass spectrometry

Ostrom, Peggy H.; Schall, Michael; Gandhi, Hasand; Shen, T. L.; Hauschka, Peter V.; Strahler, John R.; Gage, Douglas A.

doi:10.1016/s0016-7037(99)00381-6

Cited by 87 publications

(58 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Identification of these proteins is consistent with our hypothesis that this sample was derived, at least in part, from the connective tissue meninges. The second most abundant bone protein (2,6,65) osteocalcin (BGLAP), was identified here by all of the software packages used for searching (Table I). We identified 25 of 49 residues from the carboxy-terminus, with the region containing the namesake gamma-carboxyglutamic acid (gla) residues missing.…”

Section: Table I Proteins Identified In Ice Age Bison Skull (Identifimentioning

confidence: 99%

“…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)(2)(3)(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).…”

mentioning

confidence: 99%

“…Indeed, the survival of collagen, which is considered to be the most abundant bone protein, is estimated to be in the range 340 ky at 20°C. Similarly, osteocalcin, the second-most abundant bone protein, can persist for Ϸ45 ky at 20°C, thus opening an unprecedented analytical window to study extremely old samples (2,4,23).…”

mentioning

confidence: 99%

“…In the past, mass spectrometry has been used to obtain MS signals consistent with modern osteocalcin samples (2,47), and eventually postsource decay peptide fragmentation was used to confirm the identification of osteocalcin in fossil hominids dating back ϳ75 ky (48). More recently, modern "bottom-up" proteomic methods were applied to mastodon and T. rex samples (10), complementing immunohistochemistry evidence (13,17).…”

mentioning

confidence: 99%

See 3 more Smart Citations

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

View full text Add to dashboard Cite

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

Section: Table I Proteins Identified In Ice Age Bison Skull (Identifimentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

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

View full text Add to dashboard Cite

show abstract

“…It has been proposed as an alternative to collagen for dating (Ajie et al 1990(Ajie et al , 1991(Ajie et al , 1992Huq et al 1990), although with questionable success (Taylor and Hare 1995). The small size and diagenetic stability of this molecule (imparted by its packaging in bone; Collins et al 2000) is apparently ideal for exploiting the technology of proteomics to extend sequencing of biomolecules into deep time (Ostrom et al 2000).…”

Section: The Organization Of Bonementioning

confidence: 99%

The survival of organic matter in bone: a review

et al. 2002

View full text Add to dashboard Cite

show abstract

Chemical Methods in Archaeology

Spoto¹

2013

Kirk-Othmer Encyclopedia of Chemical Technology

View full text Add to dashboard Cite

Chemistry plays an important role in the study of archaeological materials. Chemistry has developed methods to date archaeological material. It has also allowed us to infer trade routes by studying ancient artifacts and also shed light on the technology used to make them. The diet and customs of ancient peoples have also been discovered by applying chemical methods. Chemistry also intervenes in the understanding of the mechanisms that cause archaeological material to degrade.The modern analytical methods available today have been used to study a wide range of archaeological inorganic, organic, and biological materials. A short overview of some of the most relevant achievements reached by applying chemical methods to archaeology is reported here.

show abstract

New strategies for characterizing ancient proteins using matrix-assisted laser desorption ionization mass spectrometry

Cited by 87 publications

References 41 publications

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

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

The survival of organic matter in bone: a review

Chemical Methods in Archaeology

Contact Info

Product

Resources

About