Premium
Two‐dimensional electrophoresis study of in vitro pellicle formation and dental caries susceptibility
Author(s) -
Vitorino Rui,
De Morais Guedes Sofia,
Ferreira Rita,
Lobo Maria João C.,
Duarte José,
FerrerCorreia António J.,
Tomer Kenneth B.,
Domingues Pedro M.,
Amado Francisco M. L.
Publication year - 2006
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.2006.00328.x
Subject(s) - saliva , lactoferrin , salivary proteins , chemistry , cystatin , in vitro , cystatin c , biochemistry , renal function
In the present study, a proteomic approach was applied to evaluate the influence of salivary protein composition on in vitro dental pellicle formation and its possible correlation with dental caries. Whole saliva, collected from caries‐free and caries‐susceptible subjects, was analyzed by two‐dimensional electrophoresis, and protein spots were identified by mass spectrometry. Data analysis of salivary protein composition showed a statistically significant correlation between the quantity of acidic proline‐rich proteins (PRPs), lipocalin, cystatin SN and cystatin S, and samples from the caries‐free group of subjects [decayed, missing or filled teeth (DMFT) = 0]. Samples from subjects with a high DMFT index appear to be correlated with high levels of amylase, immunoglobulin A, and lactoferrin. In vitro pellicle‐composition experiments showed the same correlations found for whole saliva. As cystatins are known physiological inhibitors of cathepsins, the higher quantities of lipocalin, and cystatins S and SN found in the samples from the caries‐free subjects suggest that inhibition of proteolytic events on other salivary proteins may indirectly provide tooth protection. The correlation between higher levels of the phosphorylated acidic PRPs 1/2 with samples from the caries‐free group also suggests a protective role for these proteins.