Cited by 104Calcium Carbonate Crystallization and InhibitionCoral and Marine Ecosystems StudiesOcean Acidification Effects and Responses

The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.

Immunolocalization of skeletal matrix proteins in tissue and mineral of the coral Stylophora pistillata

Open access
Mass, Tali, Drake, Jeana L., Peters, Esther C., Jiang, Wenge, Falkowski, Paul G.·2014·Proceedings of the National Academy of Sciences

Abstract

Significance: Although various aspects of biomineralization in corals have been studied for decades, the basic mechanism responsible for the precipitation of the aragonite skeleton remains enigmatic. To address this issue, we used antibodies against key biomineralization proteins derived from the common zooxanthellate coral Stylophora pistillata to elucidate the spatial arrangement of specific skeletal matrix proteins in the skeleton and in the animal tissue. To our knowledge, our results reveal for the first time that the biomineral is produced in discrete nanoscale packages in which the secreted organic matrices remain entrapped within the crystalline units whose growth they control, leading to the formation of highly ordered, microscopic, heterologous structures, which are aggregated to form a macroscopic skeleton.

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Crossref · 10.1073/pnas.1408621111

Cites

59 of 59 references verified0 citation errors · 0 not checkable

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  • Previous studies have demonstrated that acidic proteins promote calcium carbonate nucleation when on solid templates and inhibit crystal growth in solution.

    “Previous studies have demonstrated that acidic proteins promote calcium carbonate nucleation when on solid templates and inhibit crystal growth in solution.26,37−40”

    From Organic Controls over Biomineral Ca-Mg Carbonate Compositions and Morphologies (2023) · cites this paper as [26]

    The Discussion (page unavailable) proposes that coral acid-rich proteins CARPs 1 and 4 form crystal-binding substrates that lead to calcium carbonate nucleation. It does not report that acidic proteins inhibit crystal growth in solution, and presents the nucleation role as a working model rather than a demonstrated result. (LLM, conf=0.85)

    Experimental — accuracy not yet measured
  • Some biomineral species display different amino acid compositions in aragonite versus calcite regions of coral skeletons and mollusk shells.

    “Some biomineral species even display different amino acid compositions in aragonite versus calcite regions of coral skeletons4 and mollusks shells.26−28”

    From Organic Controls over Biomineral Ca-Mg Carbonate Compositions and Morphologies (2023) · cites this paper as [26]

    Citation 4 is attached to the coral-skeleton part of the sentence. The paper’s Discussion describes where different proteins occur within a coral skeleton, and its introductory passage identifies the mineral as aragonite, but neither compares aragonite with calcite regions nor reports their amino acid compositions (searched: amino acid composition, aragonite, calcite). The mollusk-shell portion is attributed to other citations. (LLM, conf=0.75)

    Experimental — accuracy not yet measured
  • Organisms that utilize both aragonite and calcite in their hard parts have higher Asp and Glu content in the calcitic regions and lower acidic amino acid contents in the aragonitic regions.

    “By comparing the mineralogy of biocarbonates and the composition of amino acids reported in the literature, we observe that organisms that utilize both aragonite and calcite in their hard parts (skeletons, shells, etc.) have higher Asp and Glu content in the calcitic regions and lower acidic amino acid contents in the aragonitic regions4,26,48,72,73 (Figure 7).”

    From Organic Controls over Biomineral Ca-Mg Carbonate Compositions and Morphologies (2023) · cites this paper as [26]

    The introduction describes acid-rich proteins in the aragonitic skeleton of Stylophora pistillata, and the Discussion describes where those proteins occur. Neither section compares Asp or Glu content between calcitic and aragonitic regions. Searches for that comparison found no passage addressing the claimed pattern. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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Citations

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Research works printed but not linked: 2

  1. DG Fautin, RN Mariscal, Cnidaria: Anthozoa. Microscopic Anatomy of Invertebrates: Placozoa, Porifera, Cnidaria, and Ctenophora, eds FW Harrison, JA Westfall (Wiley-Liss, New York) Vol 2, 267–358 (1991).
  2. EC Peters, Anatomy. Diseases of Corals, eds C Downs, C Woodley, J Porter, A Bruckner (Blackwell, Oxford, , in press.

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Metadata

Authors
Mass, T., Drake, J. L., Peters, E. C., Jiang, W., & Falkowski, P. G.
Affiliations
  • Rutgers, The State University of New Jersey (US)
  • George Mason University (US)
  • McGill University (CA)
Venue
Proceedings of the National Academy of Sciences
Published
2014-08-19
Volume
111
Issue
35
Pages
12728-12733
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2027705102
Cited by
104
References
59
Citations by year
2026: 3 · 2025: 8 · 2024: 6 · 2023: 2 · 2022: 12 · 2021: 13 · 2020: 11 · 2019: 11 · 2018: 5 · 2017: 13 · 2016: 13 · 2015: 7
FWCI
4.17
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation (1041143)
  • Princeton University
  • Rutgers Cancer Institute of New Jersey
Topics
  • Physical Sciences › Materials Science › Biomaterials › Calcium Carbonate Crystallization and Inhibition
  • Physical Sciences › Environmental Science › Ecology › Coral and Marine Ecosystems Studies
  • Physical Sciences › Earth and Planetary Sciences › Oceanography › Ocean Acidification Effects and Responses
Keywords
Stylophora pistillata, coral skeleton, matrix protein, calcification, zooxanthellate corals
MeSH terms
Actins, Animals, Antibodies, Calcium Carbonate, Carbonic Anhydrases, Crystallization, Immunohistochemistry, Minerals, Molecular Sequence Data, Cadherins, Microscopy, Immunoelectron, Extracellular Matrix Proteins, Anthozoa, Nanostructures

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