Quantitative study of the proportion of the pore volume of human fluorotic enamel filled by resin infiltrant.

AIM: Capillarity theory predicts that the pore volume infiltrated by a liquid in a body with tubular capillaries is directly proportional to the capillary radius. The expected volume available for infiltration is the loosely bound water volume, which can be related to the capillary radii. We tested the hypothesis that the proportion of the pore volume infiltrated by resin infiltrant (Vratioresin) is correlated and agrees with the proportion of the pore volume with loosely bound water ( [Formula: see text] ). DESIGN: Seven human fluorotic third molars (4 unerupted and 3 erupted; TF scores 4 to 7; fluoride content of inner coronal dentin ranged from 143 to 934µg Fluoride/g) were prepared and resin infiltration was performed during 10min in fluorotic enamel ground sections. Penetration depths were measured (polarizing microscopy and CLSM) and mineral volume and non-mineral volumes were measured at histological points (n=92) along transversal lines traced from the enamel surface to the enamel-dentin junction. RESULTS: No well-mineralized surface layer was found. Infiltration depths ranged from 250µm to 900µm. Vratioresin ranged from 1.8 to 17.7% (mean of 10.13%±4.1%), was lower than [Formula: see text] (p<0.00001 Hedge's g=1.51, 95% CI: 1.18/1.83), and correlated positively with [Formula: see text] (R=0.684; 95% CI: 0.557/0.780) and negatively with the air volume remained after infiltration (R=-0.79; 95% CI: -0.698/-0.780). [Formula: see text] exceeded Vratioresin in 5% (1/4 of [Formula: see text] ) on average. CONCLUSION: [Formula: see text] and Vratioresin correlated well, but lacked good agreement. Organic matter, firmly bound water and air remained in enamel pores after resin infiltration.

Peptide Characterization of Mature Fluorotic and Control Human Enamel.

Exposure to high fluoride levels during amelogenesis causes enamel fluorosis. This study aimed to determine and compare the amino acid sequences in the enamel of fluorotic and control teeth. This investigation included enamel samples obtained from erupted and non-erupted third molars with either TF grade 4-6 (n=7) fluorosis or no sign of fluorosis (controls, n=7). The samples were kept frozen at -20 °C until protein extraction. Samples were etched and processed with a cocktail of proteinase inhibitors and immediately analyzed. Matrix Assisted Laser Desorption/Ionization-Time-Of-Flight/Time-of-Flight Mass Spectrometry (MALDI-TOF/TOF) followed by MASCOT search aided the peptides analysis. The more abundant peptides bore the N-terminal amelogenin sequences WYQSIRPPYP (which is specific for the X-encoded amelogenin) and MPLPPHPGHPGYINF (which does not show sexual dimorphism) were not different in control or fluorotic enamel. There was no missing proteolytic cleavage in the fluorotic samples, which suggested that the increased amount of protein described in fluorotic enamel did not stem from the decreased ability of proteinases to cleave the proteins in humans. This study showed how to successfully obtain peptide from superficial enamel. A relatively low number of teeth was sufficient to provide good data on the actual peptides found in mature enamel.

Peptide Characterization of Mature Fluorotic and Control Human Enamel

Abstract Exposure to high fluoride levels during amelogenesis causes enamel fluorosis. This study aimed to determine and compare the amino acid sequences in the enamel of fluorotic and control teeth. This investigation included enamel samples obtained from erupted and non-erupted third molars with either TF grade 4-6 (n=7) fluorosis or no sign of fluorosis (controls, n=7). The samples were kept frozen at -20 °C until protein extraction. Samples were etched and processed with a cocktail of proteinase inhibitors and immediately analyzed. Matrix Assisted Laser Desorption/Ionization-Time-Of-Flight/Time-of-Flight Mass Spectrometry (MALDI-TOF/TOF) followed by MASCOT search aided the peptides analysis. The more abundant peptides bore the N-terminal amelogenin sequences WYQSIRPPYP (which is specific for the X-encoded amelogenin) and MPLPPHPGHPGYINF (which does not show sexual dimorphism) were not different in control or fluorotic enamel. There was no missing proteolytic cleavage in the fluorotic samples, which suggested that the increased amount of protein described in fluorotic enamel did not stem from the decreased ability of proteinases to cleave the proteins in humans. This study showed how to successfully obtain peptide from superficial enamel. A relatively low number of teeth was sufficient to provide good data on the actual peptides found in mature enamel.

Resumo Exposição a altos níveis de flúor durante a amelogênese causa fluorose no esmalte. Este estudo tem como objetivo determinar e comparar as sequências de aminoácidos presentes no esmalte de dentes controles e fluoróticos. A investigação incluiu amostras de esmalte obtidas de terceiros molares erupcionados e não erupcionados, ambas ou com grau de fluorose TF 4-6 (n=7) ou sem sinais de fluorose (controles, n=7), congelados a -20 oC até a extração das proteínas. As amostras sofreram ataque ácido e foram processadas utilizando um coquetel de inibidores de proteinases, sendo imediatamente analisadas. MALDI-TOF/TOF seguido pela pesquisa com MASCOT foram utilizados para a análise dos peptídeos. Os peptídeos mais abundantes foram das amelogeninas com sequências N-terminal WYQSIRPPYP (que é codificada especificamente pela amelogenina X) e MPLPPHPGHPGYINF (que não apresenta dimorfismo sexual algum), não havendo diferenças entre dentes fluoróticos e controles. Nenhuma alteração na proteólise ocorreu nas amostras fluoróticas, o que sugere que o aumento na quantidade de proteínas existentes nas amostras fluoróticas não está correlacionada a habilidade das proteinases em clivar as proteínas em humanos. Este estudo mostrou como extrair com sucesso peptídeos do esmalte superficial. Um número relativamente baixo de dentes foram suficientes para se obter ótimos dados a respeito de peptídeos encontrados no esmalte maduro.