Document Detail


Leucine-rich amelogenin peptides regulate mineralization in vitro.
MedLine Citation:
PMID:  21653221     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Amelogenin's capacity to regulate enamel formation is related to its conserved N- and C-terminal domains, its ability to self-assemble, and its ability to stabilize amorphous calcium phosphate (ACP) - a capacity enhanced by amelogenin phosphorylation. This in vitro study provides further insight into amelogenin function, using variations of the Leucine-Rich Amelogenin Peptide (LRAP), an alternative splice product comprised solely of amelogenin's N- and C-terminal domains. Peptide self-assembly was studied by dynamic light-scattering and transmission electron microscopy (TEM). TEM, selected area electron diffraction, and Fourier transform-infrared spectroscopy were also used to determine the effect of phosphorylated and non-phosphorylated LRAP on calcium phosphate formation. Results show that phosphorylated and non-phosphorylated LRAP can self-assemble into chain-like structures in a fashion dependent on the C-terminal domain. Notably, this capacity was enhanced by added calcium and to a much greater degree for phosphorylated LRAP. Furthermore, phosphorylated LRAP was found to stabilize ACP and prevent its transformation to hydroxyapatite (HA), while aligned HA crystals formed in the presence of non-phosphorylated LRAP. The N- and C-terminal amelogenin domains in non-phosphorylated LRAP are, therefore, sufficient to guide ACP transformation into ordered bundles of apatite crystals, making LRAP an excellent candidate for biomimetic approaches for enamel regeneration.
Authors:
E Le Norcy; S-Y Kwak; F B Wiedemann-Bidlack; E Beniash; Y Yamakoshi; J P Simmer; H C Margolis
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-06-07
Journal Detail:
Title:  Journal of dental research     Volume:  90     ISSN:  1544-0591     ISO Abbreviation:  J. Dent. Res.     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-08-16     Completed Date:  2011-10-13     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  0354343     Medline TA:  J Dent Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1091-7     Citation Subset:  D; IM    
Affiliation:
Department of Biomineralization, The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA.
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MeSH Terms
Descriptor/Qualifier:
Amelogenesis*
Amelogenin / chemistry
Amino Acid Sequence
Animals
Calcium Phosphates / metabolism*
Dental Enamel Proteins / chemistry*,  physiology*
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Microscopy, Electron, Transmission
Molecular Sequence Data
Nanoparticles
Phosphorylation
Protein Structure, Tertiary
Spectroscopy, Fourier Transform Infrared
Swine
Tooth Calcification / physiology*
Grant Support
ID/Acronym/Agency:
R01-DE016376/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Amelogenin; 0/Calcium Phosphates; 0/Dental Enamel Proteins; 0/amorphous calcium phosphate; 0/leucine-rich amelogenin peptide
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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