Microspectroscopic evidence of cretaceous bone proteins.
(2011) In PLoS ONE 6(4).- Abstract
- Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular preservation over deep time, has not been performed. Here, we demonstrate that endogenous proteinaceous molecules are retained in a humerus from a Late Cretaceous mosasaur (an extinct giant marine lizard). In situ immunofluorescence of demineralized bone extracts shows reactivity to antibodies raised against type I collagen, and amino acid analyses of soluble proteins extracted from the bone exhibit a composition indicative of structural proteins... (More)
- Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular preservation over deep time, has not been performed. Here, we demonstrate that endogenous proteinaceous molecules are retained in a humerus from a Late Cretaceous mosasaur (an extinct giant marine lizard). In situ immunofluorescence of demineralized bone extracts shows reactivity to antibodies raised against type I collagen, and amino acid analyses of soluble proteins extracted from the bone exhibit a composition indicative of structural proteins or their breakdown products. These data are corroborated by synchrotron radiation-based infrared microspectroscopic studies demonstrating that amino acid containing matter is located in bone matrix fibrils that express imprints of the characteristic 67 nm D-periodicity typical of collagen. Moreover, the fibrils differ significantly in spectral signature from those of potential modern bacterial contaminants, such as biofilms and collagen-like proteins. Thus, the preservation of primary soft tissues and biomolecules is not limited to large-sized bones buried in fluvial sandstone environments, but also occurs in relatively small-sized skeletal elements deposited in marine sediments. (Less)
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https://lup.lub.lu.se/record/1972940
- author
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 6
- issue
- 4
- article number
- e19445
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- wos:000290024700174
- pmid:21559386
- scopus:79955768455
- pmid:21559386
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0019445
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (BMC) (013024020), Max-laboratory (011012005), Lithosphere and Biosphere Science (011006002), Organic chemistry (S/LTH) (011001240), Functional Zoology (432112239), Department of Chemistry (011001220), Cell Pathology (013031400), Chemical Physics (S) (011001060)
- id
- 647cbc2c-2d94-4608-aed4-2026f51384e8 (old id 1972940)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21559386?dopt=Abstract
- date added to LUP
- 2016-04-01 13:13:24
- date last changed
- 2023-05-04 16:11:22
@article{647cbc2c-2d94-4608-aed4-2026f51384e8,
abstract = {{Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular preservation over deep time, has not been performed. Here, we demonstrate that endogenous proteinaceous molecules are retained in a humerus from a Late Cretaceous mosasaur (an extinct giant marine lizard). In situ immunofluorescence of demineralized bone extracts shows reactivity to antibodies raised against type I collagen, and amino acid analyses of soluble proteins extracted from the bone exhibit a composition indicative of structural proteins or their breakdown products. These data are corroborated by synchrotron radiation-based infrared microspectroscopic studies demonstrating that amino acid containing matter is located in bone matrix fibrils that express imprints of the characteristic 67 nm D-periodicity typical of collagen. Moreover, the fibrils differ significantly in spectral signature from those of potential modern bacterial contaminants, such as biofilms and collagen-like proteins. Thus, the preservation of primary soft tissues and biomolecules is not limited to large-sized bones buried in fluvial sandstone environments, but also occurs in relatively small-sized skeletal elements deposited in marine sediments.}},
author = {{Lindgren, Johan and Uvdal, Per and Engdahl, Anders and Lee, Andrew H and Alwmark, Carl and Bergquist, Karl-Erik and Nilsson, Einar and Ekström, Peter and Rasmussen, Magnus and Douglas, Desiree and Polcyn, Michael J and Jacobs, Louis L}},
issn = {{1932-6203}},
language = {{eng}},
number = {{4}},
publisher = {{Public Library of Science (PLoS)}},
series = {{PLoS ONE}},
title = {{Microspectroscopic evidence of cretaceous bone proteins.}},
url = {{https://lup.lub.lu.se/search/files/3238028/1975834.pdf}},
doi = {{10.1371/journal.pone.0019445}},
volume = {{6}},
year = {{2011}},
}