Histatin 1 Resists Proteolytic Degradation When Adsorbed to Hydroxyapatite

Authors

E. E. McDonald, The University of Western Ontario
H. A. Goldberg, The University of Western Ontario
N. Tabbara, The University of Western Ontario
F. M. Mendes, University of São Paulo, Brazil
W. L. Siqueira, The University of Western Ontario

Document Type

Article

Publication Date

2-2011

Journal

Journal of Dental Research

Volume

90

Issue

2

First Page

268

Last Page

272

URL with Digital Object Identifier

http://dx.doi.org/10.1177/0022034510388653

Abstract

Histatins are salivary proteins that exhibit a high affinity for hydroxyapatite and contribute to the acquired enamel pellicle. Previous studies have observed that, despite the high proteolytic activity in saliva, significant numbers of histatin molecules in acquired enamel pellicle are intact. Our working hypothesis was that histatins are less susceptible to proteinases present in saliva when adsorbed on the hydroxyapatite. To test this premise, we incubated histatin 1 with hydroxyapatite and human whole saliva. Proteolytic products of this incubation were then characterized by PAGE, HPLC, and mass spectrometry. This study shows for the first time that binding to hydroxyapatite confers intact histatin 1 with resistance to proteolytic degradation.