Document Detail


The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro.
MedLine Citation:
PMID:  15681234     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Amelogenin is the most abundant protein in developing dental enamel. It is believed to play an important role in the regulation of the growth and organization of enamel crystals. Amelogenin, unlike many other proteins found in biominerals, is mostly hydrophobic except for a 13 amino acid hydrophilic C-terminal domain. To clarify the role of amelogenin in enamel mineralization, we designed calcium phosphate crystal growth experiments in the presence of recombinant amelogenins with or without the charged C-terminal domain. The shape and organization of the crystals were examined by TEM in bright field and diffraction modes. It was found that both full-length and truncated amelogenin inhibit crystal growth in directions normal to the c-axis. At the same time, crystallites organized into parallel arrays only in the presence of the full-length amelogenin in monomeric form. Pre-assembled amelogenins had no effect on crystals organization. These results imply that the hydrophobic portion of amelogenin plays a role in an inhibition of crystal growth, whereas the C-terminal domain is essential for the alignment of crystals into parallel arrays. Our data also suggest that nascent enamel structure emerges as a result of cooperative interactions between forming crystals and assembling proteins.
Authors:
Elia Beniash; James P Simmer; Henry C Margolis
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of structural biology     Volume:  149     ISSN:  1047-8477     ISO Abbreviation:  J. Struct. Biol.     Publication Date:  2005 Feb 
Date Detail:
Created Date:  2005-01-31     Completed Date:  2005-06-08     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9011206     Medline TA:  J Struct Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  182-90     Citation Subset:  IM    
Affiliation:
Department of Biomineralization, The Forsyth Institute, Boston, MA 02115-3799, USA. ebeniash@forsyth.org
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MeSH Terms
Descriptor/Qualifier:
Amelogenin
Amino Acid Sequence
Animals
Calcium Phosphates / chemistry
Crystallization
Dental Enamel / chemistry
Dental Enamel Proteins / chemistry,  genetics,  metabolism*,  ultrastructure
Durapatite / chemistry*
Hydrophobicity
Mice
Molecular Sequence Data
Nanotubes / ultrastructure
Protein Structure, Tertiary
Recombinant Proteins / chemistry,  metabolism,  ultrastructure
Grant Support
ID/Acronym/Agency:
DE-13237/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Amelogenin; 0/Amelx protein, mouse; 0/Calcium Phosphates; 0/Dental Enamel Proteins; 0/Recombinant Proteins; 1306-06-5/Durapatite

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


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