RESUMEN
The link between salivary composition and sensitivity to astringency as a function of age has still not been established. In this work, we propose the hypothesis that ageing leads to changes in the concentration of salivary proline-rich proteins (PRPs), which alters the astringency perception threshold with age. To test this hypothesis, astringency sensitivity to tannic acid and saliva was assessed in 30 elderly people and 24 young people. Basic PRPs (bPRPs) and glycosylated PRPs (gPRPs) were quantified immunochemically via western blot analysis. The results showed that the amounts of bPRPs and gPRPs were similar between the young and elderly groups. However, a positive correlation between the gPRP amount and astringency threshold was observed only in the young group, while a negative correlation between the bPRP amount and astringency threshold was observed only in the elderly group. This finding suggests differences in the contribution of PRP type to astringency perception as a function of age.
RESUMEN
The mucosal pellicle (MP) is a biological film protecting the oral mucosa. It is composed of bounded salivary proteins and transmembrane mucin MUC1 expressed by oral epithelial cells. Previous research indicates that MUC1 expression enhances the binding of the main salivary protein forming the MP, MUC5B. This study investigated the influence of MUC1 structure on MP formation. A TR146 cell line, which does not express MUC1 natively, was stably transfected with genes coding for three MUC1 isoforms differing in the structure of the two main extracellular domains: the VNTR domain, exhibiting a variable number of tandem repeats, and the SEA domain, maintaining the two bound subunits of MUC1. Semi-quantification of MUC1 using dot blot chemiluminescence showed comparable expression levels in all transfected cell lines. Semi-quantification of MUC5B by immunostaining after incubation with saliva revealed that MUC1 expression significantly increased MUC5B adsorption. Neither the VNTR domain nor the SEA domain was influenced MUC5B anchoring, suggesting the key role of the MUC1 N-terminal domain. AFM-IR nanospectroscopy revealed discernible shifts indicative of changes in the chemical properties at the cell surface due to the expression of the MUC1 isoform. Furthermore, the observed chemical shifts suggest the involvement of hydrophobic effects in the interaction between MUC1 and salivary proteins.