title: Two-dimensional electrophoresis study of in vitro pellicle formation and dental caries susceptibility.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Aveiro, Portugal.
authors.forename: Rui
authors.initials: R
authors.lastname: Vitorino
authors.forename: Sofia
authors.initials: S
authors.lastname: de Morais Guedes
authors.forename: Rita
authors.initials: R
authors.lastname: Ferreira
authors.forename: Maria João C
authors.initials: MJ
authors.lastname: Lobo
authors.forename: José
authors.initials: J
authors.lastname: Duarte
authors.forename: António J
authors.initials: AJ
authors.lastname: Ferrer-Correia
authors.forename: Kenneth B
authors.initials: KB
authors.lastname: Tomer
authors.forename: Pedro M
authors.initials: PM
authors.lastname: Domingues
authors.forename: Francisco M L
authors.initials: FM
authors.lastname: Amado
mesh_terms: D000293:Adolescent; D000328:Adult; D000681:Amylases / Q000032:analysis; D002352:Carrier Proteins / Q000032:analysis; D015891:Cystatins / Q000032:analysis; D015853:Cysteine Proteinase Inhibitors / Q000032:analysis; D004245:DMF Index; D003731:Dental Caries / Q000378:metabolism; D003733:Dental Caries Susceptibility; D044622:Dental Pellicle / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007071:Immunoglobulin A, Secretory / Q000032:analysis; D007781:Lactoferrin / Q000032:analysis; D054835:Lipocalin 1; D008297:Male; D013058:Mass Spectrometry; D010455:Peptides / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis; D011392:Proline / Q000032:analysis; D055232:Proline-Rich Protein Domains; D020543:Proteome / Q000032:analysis; D055333:Salivary Cystatins; D012471:Salivary Proteins and Peptides / Q000032:analysis
chemical_list: C525171:CST1 protein, human; C525173:CST4 protein, human; D002352:Carrier Proteins; D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D007071:Immunoglobulin A, Secretory; C518443:LCN1 protein, human; D054835:Lipocalin 1; D010455:Peptides; D010750:Phosphoproteins; D020543:Proteome; D055333:Salivary Cystatins; D012471:Salivary Proteins and Peptides; D011392:Proline; D000681:Amylases; D007781:Lactoferrin