The low-molecular-weight components of human saliva remain poorly characterized. Therefore, low-molecular-weight peptides (Mr < 3000) have been purified from human parotid saliva and characterized with respect to their amino acid sequence. From the sequences obtained, it is likely that these peptides are derived from proteolysis of the hydroxyapatite-interactive human salivary proteins, histatins, proline-rich proteins, and statherins. Since human parotid saliva is an amicrobial fluid, much of the low-molecular-weight peptide fraction of this secretion appears to be derived from the proteolytic processing of the larger proteins. Because of their small size, these peptides are likely to be in exchange with dental plaque fluid and may therefore help modulate events such as demineralization/remineralization, microbial attachment, and dental plaque metabolism at the tooth-saliva interface.
Atkinson JA, Yeh C., Oppenheim FG, Bermudez D., Baum BJ, Fox PC (1990). Elevation of salivary antimicrobial proteins following HIV-I infection. J Acq Imm Def Sym3:41-48.
2.
Baum BJ, Bird JL, Millar DB, Longton RW (1976). Studies on histidine-rich polypeptides from human parotid saliva. Arch Biochem Biophys177:427-436.
3.
Bowen WH, Tabak LA , editors (1993). Cariology for the nineties . Rochester, NY: University of Rochester Press.
4.
Distler W., Kroncke A. (1987). Biologically-active, low-molecular-weight peptides in human saliva. J Dent Res66:603-604.
5.
Douglass J., Civelli O., Herbert E. (1984). Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Ann Rev Biochem53:665-715.
6.
Gibbons RJ, Hay DI, Schlesinger DH (1991). Delineation of a segment of adsorbed salivary acidic proline-rich proteins which promote adhesion of Streptococcus gordonii to apatitic surfaces. Infect Immun59:2948-2954.
7.
Hagen FK, VanWuyckhuyse B., Tabak LA (1993). Purification, cloning, and expression of a bovine UDP-GaINAc:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem2268:18960-18965.
8.
Hay DI, Smith DJ, Schluckebier SK, Moreno EC (1984). Relationship between concentration of human salivary statherin and inhibition of calcium phosphate precipitation in stimulated human parotid saliva. J Dent Res63:857-863.
9.
Hay DI, Bennick A., Schlesinger DH, Minaguchi K., Madapallimattam G., Schluckebier SK (1988). The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s, and PIF-f). Biochem J255:15-21.
10.
Holbrook IB, Molan PC (1975). The identification of a peptide in human parotid saliva particularly active in enhancing the glycolytic activity of the salivary microorganisms. Biochem J149:489-492.
11.
Isemura S., Saitoh E., Sanada K. (1980). The amino acid sequence of a salivary proline-rich peptide, P-C, and its relation to a salivary proline-rich phosphoprotein. J Biochem87:1071-1077.
12.
Jensen JL, Lamkin MS, Troxler RF, Oppenheim FG (1991). Multiple forms of statherin in human salivary secretions. Arch Oral Biol36:529-534.
13.
Kauffman DL, Bennick A., Blum M., Keller PJ (1991). Basic proline-rich proteins from human parotid saliva: relationships of the covalent structures of ten proteins from a single individual. Biochemistry30:3351-3356.
14.
Kleinberg I., Kanapka JA, Craw D. ( 1976). Effect of saliva and salivary factors on the metabolism of the mixed oral flora. In: Microbial aspects of dental caries . Proceedings of a Workshop on Microbial Aspects of Dental Caries, June 21-24, 1976, St. Simons Island, GA. Stiles HM, Loesche WJ, O'Brien TC , editors. Washington, DC: Information Retrieval Inc., Sp. Suppl. Microbiol Abstr 11:433-464.
15.
Korayem M., Westbay G., Kleinberg I. (1990). Constituents of salivary supernatant responsible for stimulation of oxygen uptake by the bacteria in human salivary sediment . Arch Oral Biol35:145-152.
Madapallimattam G., Bennick A. (1990). Phosphopeptides derived from human salivary acidic proline-rich proteins. Biological activities and concentration in saliva. Biochem J270:297-304.
18.
Makinen KK (1989). Salivary enzymes. In: Human saliva: Clinical chemistry and microbiology. Vol. II. Tenovuo JD, editor. Boca Raton, FL: CRC Press, pp. 94-119.
19.
Mandel ID, Bennick A. (1982). Quantitation of acidic proline-rich proteins in oral diseases. J Dent Res62:943-945.
20.
Margolis HC (1993). Enamel-plaque fluid interactions. In: Cariology for the nineties. Bowen WH, Tabak LA, editors. Rochester, NY: University of Rochester Press, pp. 173-186.
21.
Marquis RE, Burne RA, Parsons DT, Casiano-Colon AE (1993). Arginine deiminase and alkali generation in plaque . In: Cariology for the nineties. Bowen WH, Tabak LA, editors. Rochester, NY: University of Rochester Press, pp. 309-317.
22.
Richardson CF, Johnsson M., Raj PA, Levine MJ, Nancollas GH (1993). The influence of histatin-5 fragments on the mineralization of hydroxyapatite. Arch Oral Biol38:997-1002.
23.
Robinson R., Kauffman DL, Waye MMY, Blum M., Bennick A., Keller PJ (1989). Primary structure and possible origin of the non-glycosylated basic proline-rich protein of human submandibular/sublingual saliva. Biochem J263:497-503.
24.
Rogers AH, Zilm PS, Gully NJ, Pfennig AL (1988). Response of a Streptococcus sanguis strain to arginine-containing peptides. Infect Immun56:687-692.
25.
Schwartz SS, Hay DI, Schluckebier SK (1992). Inhibition of calcium phosphate precipitation by human salivary statherin: structure-activity relationships. Calcif Tissue Int50:511-517.
26.
Tabak LA, Bowen WH (1989). The roles of saliva (pellicle), diet and nutrition on plaque formation. J Dent Res68:1560-1566.
27.
Tabak LA, Mandel ID, Karlan D., Baurmash H. (1978). Alterations in lactoferrin concentrations in diseases of the salivary gland. J Dent Res57:43-47.
28.
Tatevossian A. (1990). Facts and artifacts in research on human dental plaque fluid. J Dent Res69:1309-1315.
29.
Troxler RF, Offner GD, Xu T., Vanderspek JC, Oppenheim FG (1990). Structural relationship between human salivary histatins. J Dent Res69:2-6.
30.
Xu L., Lal K., Santarpia RP III, Pollock JJ (1993). Salivary proteolysis of histidine-rich polypeptides and the antifungal activity of peptide degradation products. Arch Oral Biol38:277-283.
