RESUMO
PURPOSE: The aim of this study was to evaluate whether the drilling speed used during implant site preparation influences primary stability. MATERIALS AND METHODS: Eighty tapered designed implants (3.8 × 10 mm) were inserted following osteotomies created in solid rigid polyurethane foam (simulating bone type II) and cellular rigid polyurethane foam (simulating bone type IV). Half were prepared using drilling speeds of 800 rpm (low speed), and the other half were prepared using speeds of 1,500 rpm (high speed). Following insertion, implant primary stability was measured using Periotest and Osstell (resonance frequency analysis [RFA]) devices. RESULTS: Two-way analysis of variance (ANOVA) used for this study found that the drilling speed used to create the osteotomies appeared to have no significant impact on primary stability. CONCLUSION: The bone quality and not the osteotomy drilling speed seems to influence the implant primary stability.
Assuntos
Implantação Dentária Endóssea/métodos , Implantes Dentários , Retenção em Prótese Dentária/normas , Osteotomia/métodos , Análise de Variância , Implantação Dentária Endóssea/instrumentação , Planejamento de Prótese Dentária , Humanos , Modelos Teóricos , PoliuretanosRESUMO
AIM: Application of quantitative stable isotope-labelling chemistries and mass spectrometry (MS) to determine alterations in gingival crevicular fluid (GCF) proteome in periodontal disease. MATERIAL AND METHODS: Quantitative proteome of GCF from 40 healthy individuals versus 40 patients with periodontal disease was established using 320 GCF samples and stable isotope-labelling reagents, ICAT and mTRAQ, with MS technology and validated by enzyme-linked immunosorbent methods. RESULTS: We have identified 238 distinct proteins of which 180 were quantified in GCF of both healthy and periodontal patients with additional 26 and 32 distinct proteins that were found only in GCF of healthy or periodontal patients. In addition, 42 pathogenic bacterial proteins and 11 yeast proteins were quantified. The data highlighted a series of proteins not quantified previously by large-scale MS approaches in GCF with relevance to periodontal disease, such as host-derived Ig alpha-2 chain C, Kallikrein-4, S100-A9, transmembrane proteinase 13, peptidase S1 domain, several collagen types and pathogenic bacterial proteins, e.g. formamidase, leucine aminopeptidase and virulence factor OMP85. CONCLUSIONS: The innovative analytical approaches provided detailed novel changes in both host and microbial derived GCF proteomes of periodontal patients. The study defined 50 host and 16 pathogenic bacterial proteins significantly elevated in periodontal disease most of which were novel with significant potential for application in the clinical arena of periodontal disease.