Preservation of antigenic properties of macromolecules over 70 Myr

Jong, Elisabeth W. de Vrind‐de; Westbroek, Peter; Westbroek, J. F.; Bruning, J. W.

doi:10.1038/252063a0

Cited by 46 publications

(13 citation statements)

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“…The presence of amino acids in fossils has been reported subsequently by numerous investigators (2-). Peptide bonds (7,8) and even fossil organic material with preserved antigenic determinants have been reported (9). This report describes the presence of shell glycoproteins of discrete molecular weight in fossil S. thoracica that share a particular repeating amino acid sequence with their contemporary counterparts.…”

mentioning

confidence: 86%

Characterization of 80-million-year-old mollusk shell proteins.

Weiner¹,

Lowenstam²,

Hood³

1976

Proc. Natl. Acad. Sci. U.S.A.

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Fossil glycoproteins of the soluble organic matrix are present in an 80-million-year-old mollusk shell from the Late Cretaceous Period. Discrete molecular weight components, as determined by gel electrophoresis, are preserved. The fossil organic matrix was compared with the organic matrix of a living representative species of the same superfamily. A particular repeating amino acid sequence, found in contemporary mollusk shell proteins, was identified in the fossil glycoproteins. The (7,8) and even fossil organic material with preserved antigenic determinants have been reported (9). This report describes the presence of shell glycoproteins of discrete molecular weight in fossil S. thoracica that share a particular repeating amino acid sequence with their contemporary counterparts. In addition, the ultrastructure, chemistry, and mineralogy of the shell inorganic components provide information on the conditions under which the shell has been preserved. MATERIALS AND METHODSChoice of a Suitable Fossil Shell. Mollusk shells of the Late Cretaceous (Lower Maestrichtian) deposits at the Coon Creek type locality in southwestern Tennessee are well-known for their exceptional physical preservation (10, 11). Geochemical studies of the shell carbonate from a variety of species have shown that the original shell mineralogy is preserved and that strontium, magnesium, and 6180 contents of the shells have escaped detectable diagenetic alterations (12)(13)(14). We have chosen to study shells from Coon Creek of the bivalve, Scabrotrigonia thoracica. The fact that these shells still retain their original pearly luster in the nacreous layer provides additional evidence for their exceptional state of preservation. Shells of an extant representative of the superfamily Trigoniacea, Neotrigonia margaritacea, from South Australia were chosen for comparison. The Late Cretaceous trigoniacean shells were recovered from the Coon Creek deposits about 2 m below the oxidized outcrop surface. The shells'of the extant species were obtained from specimens collected alive. After removal of the soft parts, the shells were dried at room temperature.Shell Analyses. Purification of the Organic Matrix. After mechanical cleaning and removal of periostracal remnants, the shells were briefly dipped in 5.8% (wt/vol) ammonium hydroxide to remove contaminating superficial amino acids and peptides. They were then washed with redistilled water, sonicated for about a second, and then rewashed. The myostracal shell layers and hinge areas were excluded from analysis. The shells were crushed and dialyzed against 10% EDTA (wt/vol) buffered with phosphate to pH 7.0 containing small amounts of sodium azide. After decalcification, the organic matrix was dialyzed against water and Iyophilized. The insoluble fraction was removed by centrifugation, and the soluble fraction desalted on Sephadex G-25. The organic matrix of S. thoracica was almost completely soluble, whereas that of N. margaritacea was predominantly insoluble. The included Sephadex G-25 fractions ...

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mentioning

confidence: 86%

Characterization of 80-million-year-old mollusk shell proteins.

Weiner¹,

Lowenstam²,

Hood³

1976

Proc. Natl. Acad. Sci. U.S.A.

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“…DeJong et al 1974;Collins et al 1991Collins et al , 1995Collins et al , 1999Schweitzer et al 1997bSchweitzer et al , 1999aGotherstrom et al 2002;Smith et al 2005 and many others). Analyses to test this possibility are beyond the scope of this paper, which simply seeks to document the occurrence of soft tissues in fossils through time.…”

Section: Introductionmentioning

confidence: 99%

Soft tissue and cellular preservation in vertebrate skeletal elements from the Cretaceous to the present

2007

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Soft tissues and cell-like microstructures derived from skeletal elements of a well-preserved Tyrannosaurus rex (MOR 1125) were represented by four components in fragments of demineralized cortical and/or medullary bone: flexible and fibrous bone matrix; transparent, hollow and pliable blood vessels; intravascular material, including in some cases, structures morphologically reminiscent of vertebrate red blood cells; and osteocytes with intracellular contents and flexible filipodia. The present study attempts to trace the occurrence of these four components in bone from specimens spanning multiple geological time periods and varied depositional environments. At least three of the four components persist in some skeletal elements of specimens dating to the Campanian. Fibrous bone matrix is more altered over time in morphology and less likely to persist than vessels and/or osteocytes. Vessels vary greatly in preservation, even within the same specimen, with some regions retaining pliability and other regions almost crystalline. Osteocytes also vary, with some retaining long filipodia and transparency, while others present with short and stubby filipodia and deeply pigmented nuclei, or are pigmented throughout with no nucleus visible. Alternative hypotheses are considered to explain the origin/source of observed materials. Finally, a twopart mechanism, involving first cross-linking of molecular components and subsequent mineralization, is proposed to explain the surprising presence of still-soft elements in fossil bone. These results suggest that present models of fossilization processes may be incomplete and that soft tissue elements may be more commonly preserved, even in older specimens, than previously thought. Additionally, in many cases, osteocytes with defined nuclei are preserved, and may represent an important source for informative molecular data.

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“…The fossil and recent matrix proteins have similar antigenic properties indicating that the immunological properties of the original core-top 0. universa proteins are preserved. Because of the strong positive reactions, certain structures in the macromolecules must be identical (deJong et al 1974) and therefore preserved in the fossil. 4E8-3H3 monoclonal also showed strong positive reactivity with core-top planktonic foraminifer Neogloboquadrina dutertrei, although we did not have living representatives of this species to compare reactivity ofliving material.…”

Section: Discussionmentioning

confidence: 99%

Immunological and biochemical analysis of test matrix proteins in living and fossil foraminifers

Robbins

Toler

Donachy

1993

LET

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The characterization of macromolecules from shell matrix proteins in living organisms is the fundamental first step in establishing molecular phylogenies. This is particularly important if ancient macromolecules will be used for the phylogenies. Approximately 500 individuals of Orbulina universa were picked from plankton tows taken in the Gulf of Mexico during spring 1990. Proteins were extracted from the tests of the individuals, and the molecular weights of the proteins were determined and compared to 2,000–4,000‐year old samples. Gel electrophoresis of the soluble matrix (SM) from living O. universa showed at least ten protein bands, while electrophoresis of core‐top O. universa showed two protein bands. Dot‐immunobinding assays of proteins from living and fossil samples of O. universa, incubated against monoclonal antibodies raised against core‐top O. universa SM, demonstrated a reactivity with the two proteins in common. Less reactivity was obtained with living samples of the benthic foraminifers Androsina lucasi and Archaias angulatus and core‐top samples of the planktonic foraminifer Neogloboquadrina dutertrei. A partial protein sequence from one shell matrix protein approximately 65kD in size, from core‐top Orbulina universa, showed a domain of polyaspartic acid at the NH2 terminus. This is consistent with data obtained for other matrix proteins found in invertebrates and vertebrates. Sequence data provide insight into the role that the protein may play in the biomineralization of the test and will aid in modelling degradation. □Foraminifera, test proteins, monoclonal antibodies, Orbulina, Androsina, Archaias, Neogloboquadrina, biomineralization, Dot‐immunobinding assay, protein sequence.

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Preservation of antigenic properties of macromolecules over 70 Myr

Cited by 46 publications

References 1 publication

Characterization of 80-million-year-old mollusk shell proteins.

Characterization of 80-million-year-old mollusk shell proteins.

Soft tissue and cellular preservation in vertebrate skeletal elements from the Cretaceous to the present

Immunological and biochemical analysis of test matrix proteins in living and fossil foraminifers

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