Surface integrity governs the proteome of hypomineralized enamel

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. © 2010 international & american associations for dental research.