Surface integrity governs the proteome of hypomineralized enamel.

Abstract:

:Growing interest in the treatment and prevention of Molar/Incisor Hypomineralization (MIH) warrants investigation into the protein composition of hypomineralized enamel. Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent first molars using a biochemical approach. Hypomineralized enamel was found to have from 3- to 15-fold higher protein content than normal, but a near-normal level of residual amelogenins. This distinguished MIH from hypomaturation defects with high residual amelogenins (amelogenesis imperfecta, fluorosis) and so typified it as a hypocalcification defect. Second, hypomineralized enamel was found to have accumulated various proteins from oral fluid and blood, with differential incorporation depending on integrity of the enamel surface. Pathogenically, these results point to a pre-eruptive disturbance of mineralization involving albumin and, in cases with post-eruptive breakdown, subsequent protein adsorption on the exposed hydroxyapatite matrix. These insights into the pathogenesis and properties of hypomineralized enamel hold significance for prevention and treatment of MIH.

journal_name

J Dent Res

authors

Mangum JE,Crombie FA,Kilpatrick N,Manton DJ,Hubbard MJ

doi

10.1177/0022034510375824

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

1160-5

issue

10

eissn

0022-0345

issn

1544-0591

pii

0022034510375824

journal_volume

89

pub_type

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