Apatite reduces amelogenin proteolysis by MMP-20 and KLK4 in vitro.
Two enamel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation. However, the effect of hydroxyapatite (HAP) on the proteolytic activity of these enzymes remains unclear. To investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (HAP) crystals (N = 3). We found a distinct dose-dependent relationship between the amount of HAP present in the proteolysis mixture and the rate of rP172 degradation by rpMMP-20, whereas the effect of HAP on proteolysis of either rP172 or rP148 by rhKLK4 was less prominent.
Sun
Z
Z
Center for Craniofacial Molecular Biology, University of Southern California, School of Dentistry, 2250 Alcazar St., Los Angeles, CA 90033, USA.
Carpiaux
W
W
Fan
D
D
Fan
Y
Y
Lakshminarayanan
R
R
Moradian-Oldak
J
J
D000566:Amelogenesis / Q000502:physiology*; D053523:Amelogenin / Q000378:metabolism*; D000818:Animals; D017886:Durapatite / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D007610:Kallikreins / Q000378:metabolism*; D053519:Matrix Metalloproteinase 20 / Q000378:metabolism*; D020033:Protein Isoforms; D011994:Recombinant Proteins / Q000378:metabolism; D034421:Sus scrofa
D053523:Amelogenin; D020033:Protein Isoforms; D011994:Recombinant Proteins; D017886:Durapatite; D007610:Kallikreins; C120801:kallikrein 4; D053519:Matrix Metalloproteinase 20