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Amyloid-like ribbons of amelogenins in enamel mineralization

Carneiro, Karina M M ; Zhai, Halei ; Zhu, Li ; Horst, Jeremy A ; Sitlin, Melody ; Nguyen, Mychi ; Wagner, Martin ; Simpliciano, Cheryl ; Milder, Melissa and Chen, Chun-Long , et al. (2016) In Scientific Reports 6.
Abstract

Enamel, the outermost layer of teeth, is an acellular mineralized tissue that cannot regenerate; the mature tissue is composed of high aspect ratio apatite nanocrystals organized into rods and inter-rod regions. Amelogenin constitutes 90% of the protein matrix in developing enamel and plays a central role in guiding the hierarchical organization of apatite crystals observed in mature enamel. To date, a convincing link between amelogenin supramolecular structures and mature enamel has yet to be described, in part because the protein matrix is degraded during tissue maturation. Here we show compelling evidence that amelogenin self-assembles into an amyloid-like structure in vitro and in vivo. We show that enamel matrices stain positive... (More)

Enamel, the outermost layer of teeth, is an acellular mineralized tissue that cannot regenerate; the mature tissue is composed of high aspect ratio apatite nanocrystals organized into rods and inter-rod regions. Amelogenin constitutes 90% of the protein matrix in developing enamel and plays a central role in guiding the hierarchical organization of apatite crystals observed in mature enamel. To date, a convincing link between amelogenin supramolecular structures and mature enamel has yet to be described, in part because the protein matrix is degraded during tissue maturation. Here we show compelling evidence that amelogenin self-assembles into an amyloid-like structure in vitro and in vivo. We show that enamel matrices stain positive for amyloids and we identify a specific region within amelogenin that self-assembles into β-sheets. We propose that amelogenin nanoribbons template the growth of apatite mineral in human enamel. This is a paradigm shift from the current model of enamel development.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
6
article number
23105
publisher
Nature Publishing Group
external identifiers
  • pmid:27009419
  • scopus:84962291888
  • wos:000372695000001
ISSN
2045-2322
DOI
10.1038/srep23105
language
English
LU publication?
yes
id
6e1a9c9d-e8ab-4db5-9143-cbc3da5211ea
date added to LUP
2016-04-21 16:07:20
date last changed
2025-01-25 03:25:58
@article{6e1a9c9d-e8ab-4db5-9143-cbc3da5211ea,
  abstract     = {{<p>Enamel, the outermost layer of teeth, is an acellular mineralized tissue that cannot regenerate; the mature tissue is composed of high aspect ratio apatite nanocrystals organized into rods and inter-rod regions. Amelogenin constitutes 90% of the protein matrix in developing enamel and plays a central role in guiding the hierarchical organization of apatite crystals observed in mature enamel. To date, a convincing link between amelogenin supramolecular structures and mature enamel has yet to be described, in part because the protein matrix is degraded during tissue maturation. Here we show compelling evidence that amelogenin self-assembles into an amyloid-like structure in vitro and in vivo. We show that enamel matrices stain positive for amyloids and we identify a specific region within amelogenin that self-assembles into β-sheets. We propose that amelogenin nanoribbons template the growth of apatite mineral in human enamel. This is a paradigm shift from the current model of enamel development.</p>}},
  author       = {{Carneiro, Karina M M and Zhai, Halei and Zhu, Li and Horst, Jeremy A and Sitlin, Melody and Nguyen, Mychi and Wagner, Martin and Simpliciano, Cheryl and Milder, Melissa and Chen, Chun-Long and Ashby, Paul and Svensson Bonde, Johan and Li, Wu and Habelitz, Stefan}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{Amyloid-like ribbons of amelogenins in enamel mineralization}},
  url          = {{http://dx.doi.org/10.1038/srep23105}},
  doi          = {{10.1038/srep23105}},
  volume       = {{6}},
  year         = {{2016}},
}