Electron-microscopic demonstration of proline-rich proteins, statherin, and histatins in acquired enamel pellicles in vitro

Citation
P. Schupbach et al., Electron-microscopic demonstration of proline-rich proteins, statherin, and histatins in acquired enamel pellicles in vitro, EUR J OR SC, 109(1), 2001, pp. 60-68
Citations number
43
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Dentistry/Oral Surgery & Medicine","da verificare
Journal title
EUROPEAN JOURNAL OF ORAL SCIENCES
ISSN journal
0909-8836 → ACNP
Volume
109
Issue
1
Year of publication
2001
Pages
60 - 68
Database
ISI
SICI code
0909-8836(200102)109:1<60:EDOPPS>2.0.ZU;2-7
Abstract
Proline-rich proteins (PRPs), histatins, and statherin are salivary protein s that exhibit high affinities for hydroxyapatite surfaces. In vitro experi ments with parotid, submandibular/sublingual or whole saliva have shown the se proteins to adsorb selectively to tooth surfaces. This investigation foc used on the histomorphological identification of PRPs, histatins, and stath erin in acquired enamel pellicles. Synthetic hydroxyapatite or bovine ename l were exposed to glandular secretions, and whole saliva and pellicle precu rsor proteins were identified immunohistologically by electron microscopy. Results obtained by back-scattered scanning electron microscopy showed thes e proteins to be present in pellicles. Pellicles displayed a distinct struc ture consisting of a sponge-like meshwork of microglobules. Interconnection s between structural elements were identified in submandibular/sublingual a nd whole saliva pellicles only. Transmission electron microscopy of pellicl es formed on bovine enamel surfaces revealed a tendency for preferential lo calization of precursor proteins within the protein film. Since the data sh owed the presence of pellicle precursors in pellicles derived both from gla ndular secretions and from whole saliva! it is likely that PRPs, histatins, and statherin are integral components of acquired enamel pellicles in vivo .