Journal of Dental Research, Vol 73, 1717-1726, Copyright © 1994 by International & American Associations for Dental Research Online Journals

ARTICLES

Human salivary acidic proline-rich protein polymorphisms and biosynthesis studied by high-performance liquid chromatography

D. I. Hay, J. M. Ahern, S. K. Schluckebier and D. H. Schlesinger
Department of Biochemistry, Forsyth Dental Center, Boston, Massachusetts 02115-3799.

Human salivary acidic proline-rich proteins (PRPs) constitute a significant fraction of the total salivary protein and possess important biological activities. Different genetic and post-translationally processed forms of the PRPs exhibit significant quantitative variations in several of these activities, especially the modulation of salivary calcium phosphate chemistry and oral bacterial adhesion. To quantify and understand these differences, we have developed a high-performance liquid chromatography (HPLC) method to identify and measure individual PRPs in saliva. The data obtained permit the identification of PRP polymorphisms and phenotypes, the determination of the relative amounts of PRPs derived from the two loci, PRH1 and PRH2, and the measurement of the extent of post-translational cleavage of the primary polypeptide products. Substantial inter-gland and inter-individual variations were found in relative amounts of PRPs derived from the two loci (at least two-fold), and in post-translational cleavage (greater than two-fold), both of which are likely to be biologically significant. Also in this study, the presence of what appear to be minor amounts of numerous variant PRPs in glandular secretions was observed, and two uncommon PRP polymorphisms were identified in the 127 subjects studied.

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