New in vitro Model for the Acquired Enamel Pellicle : Pellicles Formed from Whole Saliva Show Inter-subject Consistency in Protein Composition and Proteolytic Fragmentation Patterns

• Published in: Journal of dental research Vol. 80; no. 1; pp. 385 - 388
• Main Authors: Lamkin, M.S., Migliari, D., Yao, Y., Troxler, R.F., Oppenheim, F.G.
• Format: Journal Article
• Language: English
• Published: Los Angeles, CA SAGE Publications 01.01.2001; SAGE PUBLICATIONS, INC
• Subjects: adsorption; Adult; Amino Acid Sequence; Chromatography, Gel; Chromatography, High Pressure Liquid - methods; Dental Calculus - chemistry; Dental Pellicle; Durapatite; Humans; Hydrolysis; hydroxyapatite; pellicle; proteolysis; Saliva - chemistry; Salivary Proteins and Peptides - chemistry; Tissue Adhesions; whole saliva; hydroxyapatite; adsorption; proteolysis; whole saliva; pellicle
• ISSN: 0022-0345; 1544-0591
• DOI: 10.1177/00220345010800011501

The present investigation was undertaken to investigate the variability of proteins in whole saliva which adsorb to hydroxyapatite and are thus likely to be precursors of the acquired enamel pellicle. Whole-saliva proteins from 18 subjects were absorbed to hydroxyapatite, and the gel filtration patterns of released proteins revealed four major peaks and three minor peaks eluting between the major peaks. Amino acid analysis indicated that minor peaks contained fragments of proteins in major peaks, and this was confirmed by sequence analysis. Major peaks comprised 95% and minor peaks comprised 5% of protein absorbed to hydroxyapatite, suggesting a limited proteolytic capacity of whole saliva. HPLC elution patterns of components in minor peaks suggested that proteolysis is not totally random but is an orderly and consistent process. These studies suggest that whole saliva may be suitable as a model system for the investigation of post-secretory modifications of salivary proteins important for the formation of the acquired enamel pellicle.