4.7 Article

Mass Spectrometry and Antibody-Based Characterization of Blood Vessels from Brachylophosaurus canadensis

期刊

JOURNAL OF PROTEOME RESEARCH
卷 14, 期 12, 页码 5252-5262

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.5b00675

关键词

Brachylophosaurus canadensis; blood vessels; dinosaur; cytoskeleton; actin; tubulin; myosin; tropomyosin; tap honomy; preservation

资金

  1. NSF EAR [0541744, DGE-0750733]
  2. David and Lucile Packard Foundation
  3. NSF INSPIRE
  4. NIH [GM067193, R21GM94557]
  5. Cancer Biology Training Grant [5 T32 CA081156-08]
  6. Cancer Prevention and Research Institute of Texas
  7. Metastasis Research Center at MD Anderson Cancer Center, NIH [DK55001, DK81976, CA125550, CA155370, CA163191]
  8. Directorate For Geosciences
  9. Division Of Earth Sciences [0541744] Funding Source: National Science Foundation
  10. Division Of Earth Sciences
  11. Directorate For Geosciences [1344198] Funding Source: National Science Foundation

向作者/读者索取更多资源

Structures similar to blood vessels in location, morphology, flexibility, and transparency have been recovered after demineralization of multiple dinosaur cortical bone fragments from multiple specimens, some of which are as old as 80 Ma. These structures were hypothesized to be either endogenous to the bone (i.e., of vascular origin) or the result of biofilm colonizing the empty osteonal network after degradation of original organic components. Here, we test the hypothesis that these structures are endogenous and thus retain proteins in common with extant archosaur blood vessels that can be detected with high-resolution mass spectrometry and confirmed by irnmunofluorescence. Two lines of evidence support this hypothesis. First, peptide sequencing of Brachylophosaurus canadensis blood vessel extracts is consistent with peptides comprising extant archosaurian blood vessels and is not consistent with a bacterial, cellular slime mold, or fungal origin. Second, proteins identified by mass spectrometry can be localized to the tissues using antibodies specific to these proteins, validating their identity. Data are available via ProteomeXchange with identifier PXDO01738.

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