Changes in the composition of the acquired enamel pellicle according to its location in the oral cavity: proteomic study

• Autor(a) principal: Talita Mendes da Silva Ventura
• Data de Publicação: 2016
• Tipo de documento: Dissertação
• Idioma: eng
• Título da fonte: Biblioteca Digital de Teses e Dissertações da USP
• Texto Completo: https://doi.org/10.11606/D.25.2016.tde-12112021-105034

The acquired enamel pellicle (AEP) is a bacteria-free organic film formed in vivo as a result of selective adsorption of salivary proteins on the surface of the tooth. It also contains glycoproteins and lipids. The presence of proteins in the AEP forms a protective interface on the tooth surface that participates in the interfacial events that occur in the oral cavity. The objective of this study was to detect changes in the protein profile of the AEP formed in vivo according to its location in the dental arches. Nine volunteers, aged 18 to 35 years, non-smokers, with good general and oral health participated in the study. The acquired pellicle was formed in the morning, for 120 minutes, after prophylaxis with pumice. Pellicle formed at upper and lower anterior labial (ULALa; teeth 13-23 and 33-43), upper anterior palatal (UAPa; teeth 13-23), lower anterior lingual (LALi; teeth 33-43), upper and lower posterior labial (ULPLa; teeth 14-17 24 to 27, 34 to 37 and 44 to 47), upper posterior palatal (UPPa; teeth 14 to 17 and 24 to 27) and lower posterior lingual (LPLi; teeth 34 to 37 and 44 to 47) regions was collected separately for analysis. After its formation, the pellicle was collected with filter paper soaked in 3% citric acid and processed for analysis by LC-ESI-MS/MS. The MS/MS spectra obtained were compared with human protein databases (SWISS PROT). Label-free quantification was done using the PLGs software. A total of 363 proteins were found, of which 252 are unique proteins for one of the regions, while 25 proteins care to all of them, including Protein S100-A8, Lysozyme C, Lactoferrin, Sthatherin, Ig alpha-2 chain C, ALB protein, Myeloperoxidase and Submaxillary gland androgen-regulated protein 3B. In the quantitative analysis, 9 comparisons were made and many proteins were differently expressed among the groups, thus demonstrating that the location in the dental arches can change the composition of the AEP. Some proteins not previously found in the AEP were identified and their function in the AEP was inferred from the literature. In conclusion, the composition of the AEP changes as a function of its location in the dental arches. These data should be taken into account when we think about the protective potential of the acquired pellicle against tooth demineralization and provide important insights for understanding the differential protective roles of the AEP as a function of its location in the dental arches.