Proteomics and Coast Salish blankets: a tale of shaggy dogs?

Solazzo, Caroline; Heald, Susan; Ballard, Mary W.; Ashford, David A.; DePriest, Paula T.; Koestler, Robert J.; Collins, Matthew J.

doi:10.1017/s0003598x00062141

Cited by 60 publications

(30 citation statements)

References 18 publications

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“…Hair and wool from sheep, cashmere and mohair goat, cow, yak, camel, alpaca, angora rabbit, and dog were obtained locally from fibre suppliers and farms. Llama, vicuna, guanaco, alpaca, Bactrian camel, yak, horse, deer and reindeer were sampled from the fibre collection at the Museum Conservation Institute and the mountain goat from the Smithsonian's National Museum of Natural History (NMNH) . Mouflon (origin Poland), and baleen were available at AgResearch.…”

Section: Methodsmentioning

confidence: 99%

“…Animal fibres have recently been identified using specific peptide markers from mass spectra acquired by MALDI‐TOF‐MS (matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry); peptides are obtained after trypsin digestion of proteins and identified by their mass‐to‐charge ratio ( m/z ). The technique was successful in identifying the different elements of the clothing of Oetzi, and to prove the existence of dog hair in Coast Salish blankets . In both cases, the textiles proved to be made of a wide range of species and the proteomics approach was particularly useful in characterising blends of fibres (dog/goat or sheep/goat) in the Coast Salish textiles.…”

mentioning

confidence: 99%

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Characterisation of novel α‐keratin peptide markers for species identification in keratinous tissues using mass spectrometry

Solazzo

Wadsley

Dyer

et al. 2013

Rapid Comm Mass Spectrometry

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Characterisation of novel α‐keratin peptide markers for species identification in keratinous tissues using mass spectrometry

Solazzo

Wadsley

Dyer

et al. 2013

Rapid Comm Mass Spectrometry

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“…[49] Keratin-based species identification method Ancient proteins extracted and sequenced from fossil bones offer an extraordinary reservoir of genetic information that has recently become tractable through the application of mass spectrometric (MS) techniques. [24,27,49,50] Other sources of ancient proteins are dental pulps [51] or even contents of ceramics like amphorae. [52] Despite their potential use, hard keratins are an unexploited source of ancient proteins.…”

Section: Keratin Propertiesmentioning

confidence: 99%

“…In a slightly varied form the method was recently applied to species identification of domestic dog, sheep and goat in ancient Native Americans' woolen blankets. [50] …”

Section: Keratin Propertiesmentioning

confidence: 99%

Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry combined with multidimensional scaling, binary hierarchical cluster tree and selected diagnostic masses improves species identification of Neolithic keratin sequences from furs of the Tyrolean Iceman Oetzi

Hollemeyer

Altmeyer²,

Heinzle

et al. 2012

Rapid Comm Mass Spectrometry

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The identification of fur origins from the 5300-year-old Tyrolean Iceman's accoutrement is not yet complete, although definite identification is essential for the socio-cultural context of his epoch. Neither have all potential samples been identified so far, nor there has a consensus been reached on the species identified using the classical methods. Archaeological hair often lacks analyzable hair scale patterns in microscopic analyses and polymer chain reaction (PCR)-based techniques are often inapplicable due to the lack of amplifiable ancient DNA. To overcome these drawbacks, a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) method was used exclusively based on hair keratins. Thirteen fur specimens from his accoutrement were analyzed after tryptic digest of native hair. Peptide mass fingerprints (pmfs) from ancient samples and from reference species mostly occurring in the Alpine surroundings at his lifetime were compared to each other using multidimensional scaling and binary hierarchical cluster tree analysis. Both statistical methods highly reflect spectral similarities among pmfs as close zoological relationships. While multidimensional scaling was useful to discriminate specimens on the zoological order level, binary hierarchical cluster tree reached the family or subfamily level. Additionally, the presence and/or absence of order, family and/or species-specific diagnostic masses in their pmfs allowed the identification of mammals mostly down to single species level. Red deer was found in his shoe vamp, goat in the leggings, cattle in his shoe sole and at his quiver's closing flap as well as sheep and chamois in his coat. Canid species, like grey wolf, domestic dog or European red fox, were discovered in his leggings for the first time, but could not be differentiated to species level. This is widening the spectrum of processed fur-bearing species to at least one member of the Canidae family. His fur cap was allocated to a carnivore species, but differentiation between brown bear and a canid species could not be made with certainty.

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“…PMF has been widely used on collagen from bone and soft tissues and specimens can generally be identified at the genus level but recent studies have shown that some markers were diagnostic to the species level in certain marine mammals (Kirby et al, 2013). PMFs of keratin in animal fibers have also been successfully used to identify ancient textiles and cloths (Solazzo et al, 2011;Hollemeyer et al, 2012).…”

Section: Species Identification Of Keratins Using Peptide Mass Fingermentioning

confidence: 99%

Advances in identifying archaeological traces of horn and other keratinous hard tissues

O'Connor

Solazzo²,

Collins

2014

Studies in Conservation

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Despite being widely utilized in the production of cultural objects, keratinous hard tissues, such as horn, baleen, and tortoiseshell, rarely survive in archaeological contexts unless factors combine to inhibit biodeterioration. Even when these materials do survive, working, use, and diagenetic changes combine to make identification difficult. This paper reviews the chemistry and deterioration of keratin and past approaches to the identification of keratinous archaeological remains. It describes the formation of horn, hoof, baleen, and tortoiseshell and demonstrates how identification can be achieved by combining visual observation under low-power magnification with an understanding of the structure and characteristic deterioration of these materials. It also demonstrates how peptide mass fingerprinting of the keratin can be used to identify keratinous tissues, often to species, even when recognizable structural information has not survived.

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Proteomics and Coast Salish blankets: a tale of shaggy dogs?

Cited by 60 publications

References 18 publications

Characterisation of novel α‐keratin peptide markers for species identification in keratinous tissues using mass spectrometry

Characterisation of novel α‐keratin peptide markers for species identification in keratinous tissues using mass spectrometry

Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry combined with multidimensional scaling, binary hierarchical cluster tree and selected diagnostic masses improves species identification of Neolithic keratin sequences from furs of the Tyrolean Iceman Oetzi

Advances in identifying archaeological traces of horn and other keratinous hard tissues

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