Heritable Salivary Proteins and Dental Disease

Friedman, Robert D.; Azen, Edwin A.; Yu, Pao‐Lo; Green, P.A.; Karn, Robert C.; Merritt, A. Donald

doi:10.1159/000153161

Cited by 13 publications

(8 citation statements)

References 4 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Antibody detection is impractical, because the additional amino acid sequence that characterizes Db duplicates part of the Pa and Pif sequences (Azen et al, 1987). The findings of this study call into question the reported association of Db gene expression with greater caries experience in African-American adults (Friedman et al, 1980). Compared with African-Americans, the caries experience of Db-positive Caucasians was less in magnitude and not significant.…”

Section: Discussioncontrasting

confidence: 64%

Acidic Proline-rich Protein Db and Caries in Young Children

et al. 2007

View full text Add to dashboard Cite

Polymorphic, acidic proline-rich proteins (PRPs) in saliva influence the attachment of bacteria associated with caries. Our aims were to detect one of three acidic PRP alleles of the PRH1 locus (Db) using polymerase chain-reaction (PCR) on genomic DNA, and to determine its association with caries. DNA was obtained from buccal swabs from Caucasian and African-American children, and their caries experience was recorded. PCR primers designed around exon 3 of the PRH1 locus gave a 416-base product representing Db and a 353-base product representing the other two alleles (Pa or Pif). In Caucasians, Db gene frequency was 14%, similar to Db protein from parotid saliva. In African-Americans, however, it was 37%, 18% lower than Db from parotid saliva (reported previously). Compared with African-Americans, all Caucasians had significantly greater Streptococcus mutans colonization, but only Db-negative Caucasians had significantly more caries. Alleles linked to Db may explain racial differences in caries experience.

show abstract

Section: Discussioncontrasting

confidence: 64%

Acidic Proline-rich Protein Db and Caries in Young Children

et al. 2007

View full text Add to dashboard Cite

show abstract

“…In Db, a 63-bp sequence in exon 3 is repeated (1), making the protein about 12% longer. A. naeslundii attachment to apatite coated with Db-positive saliva is inhibited, whereas that of S. mutans is enhanced and the subjects have a significantly greater caries experience (14,42).…”

Section: Discussionmentioning

confidence: 96%

Antibody Response to Actinomyces Antigen and Dental Caries Experience: Implications for Caries Susceptibility

Levine

Owen

Avery

2005

Clin Vaccine Immunol

View full text Add to dashboard Cite

show abstract

“…In this location the PRP may also act as receptors for commensal and pathogenic organisms which colonize teeth, and recently the PRP have been identified as selective mediators of bacterial adhesion to hydroxyapatite (Gibbons & Hay, 1988a,b), which is the prototype mineral for dental enamel. This observation seems highly significant in that differences in the phenotypic expression of the PRPs have been related to variations in oral disease (Friedman et al, 1980;Yu et al, 1986). All the foregoing properties depend on structural features of the PRPs (Bennick et al, , 1981Moreno et al, 1982Moreno et al, , 1984Aoba et al, 1984;Hay et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f)

Hay

Bennick

Schlesinger

et al. 1988

Biochemical Journal

113

View full text Add to dashboard Cite

Human glandular salivary secretions contain several acidic proline-rich phosphoproteins (PRPs). These proteins have important biological functions related to providing a protective environment for the teeth, and appear to possess other activities associated with modulation of adhesion of bacteria to oral surfaces. These functions and activities depend on the primary structures of the PRPs. Previously determined amino acid sequences of two 150-residue molecules, PRP-1 and PRP-2, and two related 106-residue proteins, PRP-3 and PRP-4, indicated that residue 4 was Asn in PRP-1 and PRP-3, and Asp in PRP-2 and PRP-4, and position 50 was Asn in all four proteins. Recent data from cDNA sequence studies and further structural studies, however, showed that the previously proposed sequences cannot be completely correct. The present work has shown that the protein previously designated as PRP-1 actually consisted of two positional isomers, PIF-s, which has Asn and Asp at positions 4 and 50 respectively, and authentic PRP-1, which has the reverse arrangement. The same isomerism is present in the smaller proteins, PIF-f and PRP-3. Since the isomeric pairs have identical compositions and charges, their presence was not previously detected. Also, by using a more highly purified preparation, it has been found that position 50 in PRP-2 and PRP-4 is Asp, rather than Asn previously reported. These new findings for the six PRPs define their complete primary structures, which are now consistent with those proposed for PRP-1 and PIF-s from cDNA data, and are also consistent with the chromatographic and electrophoretic behaviours of the six PRPs and their derived peptides. These corrected structures are important for understanding the biological functions and activities of these unusual proteins.

show abstract

Heritable Salivary Proteins and Dental Disease

Cited by 13 publications

References 4 publications

Acidic Proline-rich Protein Db and Caries in Young Children

Acidic Proline-rich Protein Db and Caries in Young Children

Antibody Response to Actinomyces Antigen and Dental Caries Experience: Implications for Caries Susceptibility

The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f)

Contact Info

Product

Resources

About