Open AccessFluoride Does Not Inhibit Enamel Protease Activity
Author(s) -
Coralee E. Tye,
Jerry Antone,
John D. Bartlett
Publication year - 2010
Publication title -
journal of dental research
Language(s) - English
Resource type - Journals
eISSN - 1544-0591
pISSN - 0022-0345
DOI - 10.1177/0022034510390043
Subject(s) - enamel paint , chemistry , amelogenin , fluoride , cathepsin l , protease , biochemistry , proteolytic enzymes , cathepsin , proteases , enzyme , dentistry , medicine , inorganic chemistry , gene
Fluorosed enamel can be porous, mottled, discolored, hypomineralized, and protein-rich if the enamel matrix is not completely removed. Proteolytic processing by matrix metalloproteinase-20 (MMP20) and kallikrein-4 (KLK4) is critical for enamel formation, and homozygous mutation of either protease results in hypomineralized, protein-rich enamel. Herein, we demonstrate that the lysosomal proteinase cathepsin K is expressed in the enamel organ in a developmentally defined manner that suggests a role for cathepsin K in degrading re-absorbed enamel matrix proteins. We therefore asked if fluoride directly inhibits the activity of MMP20, KLK4, dipeptidyl peptidase I (DPPI) (an in vitro activator of KLK4), or cathepsin K. Enzyme kinetics were studied with quenched fluorescent peptides with purified enzyme in the presence of 0-10 mM NaF, and data were fit to Michaelis-Menten curves. Increasing concentrations of known inhibitors showed decreases in enzyme activity. However, concentrations of up to 10 mM NaF had no effect on KLK4, MMP20, DPPI, or cathepsin K activity. Our results show that fluoride does not directly inhibit enamel proteolytic activity.