Risk factors and longitudinal regenerative outcomes of sinus membrane perforation during lateral window sinus floor elevation: A retrospective analysis up to 9 years.

BACKGROUND: Lateral-window sinus floor elevation (LSFE) is a reliable procedure to reconstruct the posterior maxilla for implant therapy. This retrospective study aimed to investigate risk factors associated with Schneiderian membrane perforation (SMP) occurrence during LSFE and longitudinal regenerative outcomes following LSFE up to 9 years. METHODS: Patients who had LSFE between 2010 and 2019 were included. All demographic and surgical-related data were retrieved from existing electronic health records. Radiographs were used to evaluate the vertical dimensional changes of ridge and graft materials and the potential anatomic factors of SMP. RESULTS: A total of 122 LSFE procedures in 99 patients were included in the study. Mean ridge height gain and graft shrinkages were 9.5 ± 3.47 and 1.57 ± 2.85 mm. The influence of the healing period on graft shrinkage showed a positive trend; the longer the healing period, the greater the graft shrinkage (p = 0.09). The pathology in the sinus showed a positive correlation with SMP (p = 0.07). However, other anatomical factors did not negatively impact SMP and subsequent ridge height gain (p > 0.05). CONCLUSIONS: With inherent limitation, the findings with up to 9 years of follow-up indicate a consistent ridge remodeling lasting for about 3 years after LSFE procedures. SMP or membrane thickening may not significantly affect the ridge gain following LSFE. The healing period had the most significant influence on graft shrinkage, showing that the longer the healing time between LSFE and implant placement, the greater the graft shrinkage.

Control of Calcium Phosphate Nucleation and Transformation through Interactions of Enamelin and Amelogenin Exhibits the "Goldilocks Effect".

Although amelogenin comprises the vast majority of the matrix that templates calcium phosphate nucleation during enamel formation, other proteins, particularly enamelin, are also known to play an important role in the formation of enamel's intricate architecture. However, there is little understanding of the interplay between amelogenin and enamelin in controlling processes of mineral nucleation and growth. Here, we used an in vitro model to investigate the impact of enamelin interaction with amelogenin on calcium phosphate nucleation for a range of enamelin-to-amelogenin ratios. We found that amelogenin alone is a weak promoter of nucleation, but addition of enamelin enhanced nucleation rates in a highly nonlinear, nonmonotonic manner reaching a sharp maximum at a ratio of 1:50 enamelin/amelogenin. We provide a phenomenological model to explain this effect that assumes only isolated enamelin proteins can act as sites of enhanced nucleation, while enamelin oligomers cannot. Even when interaction is random, the model reproduces the observed behavior, suggesting a simple means to tightly control the timing and extent of nucleation and phase transformation by amelogenin and enamelin.

Matrix metalloproteinase-20 mediates dental enamel biomineralization by preventing protein occlusion inside apatite crystals.

Reconstruction of enamel-like materials is a central topic of research in dentistry and material sciences. The importance of precise proteolytic mechanisms in amelogenesis to form a hard tissue with more than 95% mineral content has already been reported. A mutation in the Matrix Metalloproteinase-20 (MMP-20) gene results in hypomineralized enamel that is thin, disorganized and breaks from the underlying dentin. We hypothesized that the absence of MMP-20 during amelogenesis results in the occlusion of amelogenin in the enamel hydroxyapatite crystals. We used spectroscopy and electron microscopy techniques to qualitatively and quantitatively analyze occluded proteins within the isolated enamel crystals from MMP-20 null and Wild type (WT) mice. Our results showed that the isolated enamel crystals of MMP-20 null mice had more organic macromolecules occluded inside them than enamel crystals from the WT. The crystal lattice arrangements of MMP-20 null enamel crystals analyzed by High Resolution Transmission Electron Microscopy (HRTEM) were found to be significantly different from those of the WT. Raman studies indicated that the crystallinity of the MMP-20 null enamel crystals was lower than that of the WT. In conclusion, we present a novel functional mechanism of MMP-20, specifically prevention of unwanted organic material entrapped in the forming enamel crystals, which occurs as the result of precise amelogenin cleavage. MMP-20 action guides the growth morphology of the forming hydroxyapatite crystals and enhances their crystallinity. Elucidating such molecular mechanisms can be applied in the design of novel biomaterials for future clinical applications in dental restoration or repair.

Analysis of co-assembly and co-localization of ameloblastin and amelogenin.

Epithelially-derived ameloblasts secrete extracellular matrix proteins including amelogenin, enamelin, and ameloblastin. Complex intermolecular interactions among these proteins are believed to be important in controlling enamel formation. Here we provide in vitro and in vivo evidence of co-assembly and co-localization of ameloblastin with amelogenin using both biophysical and immunohistochemical methods. We performed co-localization studies using immunofluorescence confocal microscopy with paraffin-embedded tissue sections from mandibular molars of mice at 1, 5, and 8 days of age. Commercially-available ameloblastin antibody (M300) against mouse ameloblastin residues 107-407 and an antibody against full-length recombinant mouse (rM179) amelogenin were used. Ameloblastin-M300 clearly reacted along the secretory face of ameloblasts from days 1-8. Quantitative co-localization was analyzed (QCA) in several configurations by choosing appropriate regions of interest (ROIs). Analysis of ROIs along the secretory face of ameloblasts revealed that at day 1, very high percentages of both the ameloblastin and amelogenin co-localized. At day 8 along the ameloblast cells the percentage of co-localization remained high for the ameloblastin whereas co-localization percentage was reduced for amelogenin. Analysis of the entire thickness on day 8 revealed no significant co-localization of amelogenin and ameloblastin. With the progress of amelogenesis and ameloblastin degradation, there was a segregation of ameloblastin and co-localization with the C-terminal region decreased. CD spectra indicated that structural changes in ameloblastin occurred upon addition of amelogenin. Our data suggest that amelogenin-ameloblastin complexes may be the functional entities at the early stage of enamel mineralization.