Two-dimensional electrophoresis study of in vitro pellicle formation and dental caries susceptibility

• Type: Article in International Scientific Journal
• Date: 2006

Authors

vitorino, r (Author) Other; guedes, sdm (Author) Other; ferreira, r (Author) Other; lobo, mjc (Author) Other; duarte, j (Author) FADEUP; ferrer-correia, aj (Author) Other; tomer, kb (Author) Other; domingues, pm (Author) Other; amado, fml (Author) Other

Journal

Title: European Journal of Oral Sciences

Vol. 114 No. 2

Pages: 147-153

ISSN: 0909-8836

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 79 Citations

Scopus - 84 Citations

Pubmed / Medline

Scientific classification

FOS: Medical and Health sciences > Clinical medicine

Other information

Authenticus ID: P-004-MDS

DOI: 10.1111/j.1600-0722.2006.00328.x

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7