TY - JOUR
T1 - The inhibitory effect of proanthocyanidin on soluble and collagen-bound proteases
AU - Epasinghe, Don Jeevanie
AU - Yiu, Cynthia Kar Yung
AU - Burrow, Michael Francis
AU - Hiraishi, Noriko
AU - Tay, Franklin Russell
N1 - Funding Information:
This work was supported by Grant 201011159189 , Faculty of Dentistry, The University of Hong Kong .
PY - 2013/9
Y1 - 2013/9
N2 - Objective This study evaluated the inhibitory effect of proanthocyanidin (PA), a natural collagen cross-linker, on soluble and matrix-bound proteases, which are responsible for progressive degradation of exposed collagen fibrils within the hybrid layer and resin-dentine bond failure over time. Methods The inhibitory effects of PA (1%, 2%, 3%, 4.5% and 6%) on soluble recombinant matrix metalloproteinases (MMP-2, -8 and -9) and cysteine cathepsins (cathepsin B and K) were evaluated using MMP and cysteine cathepsins fluorometric assay kits. Chlorhexidine (CHX) was used as an inhibitor control. The effect of PA on endogenous matrix-bound proteases was examined by determining the change in dry mass of demineralized dentine beams and solubilized collagen peptides over 30 days. Two-way ANOVA and Tukey multiple comparison tests were used to analyze the effect of PA and proteases on the percentage inhibition of soluble proteases (α = 0.05). Kruskal-Wallis one-way ANOVA and Dunn's multiple comparison tests were used to analyse the effect of PA on loss of dry mass and hydroxyproline content over time (α = 0.05). Results Proanthocyanidin inactivated more than 90% of soluble recombinant MMP-2, -8 and -9 and around 75-90% of cysteine cathepsin B and K, which was significantly higher than CHX (P < 0.05). The inhibition of endogenous proteases by PA increased in a dose-dependent manner. The loss of dry mass and hydroxyproline release in the medium over time was the lowest in dentine beams pretreated with PA < CHX < control (P < 0.05). Conclusion Proanthocyanidin exhibited both dentine MMP and cysteine cathepsins inhibition, which was higher than chlorhexidine.
AB - Objective This study evaluated the inhibitory effect of proanthocyanidin (PA), a natural collagen cross-linker, on soluble and matrix-bound proteases, which are responsible for progressive degradation of exposed collagen fibrils within the hybrid layer and resin-dentine bond failure over time. Methods The inhibitory effects of PA (1%, 2%, 3%, 4.5% and 6%) on soluble recombinant matrix metalloproteinases (MMP-2, -8 and -9) and cysteine cathepsins (cathepsin B and K) were evaluated using MMP and cysteine cathepsins fluorometric assay kits. Chlorhexidine (CHX) was used as an inhibitor control. The effect of PA on endogenous matrix-bound proteases was examined by determining the change in dry mass of demineralized dentine beams and solubilized collagen peptides over 30 days. Two-way ANOVA and Tukey multiple comparison tests were used to analyze the effect of PA and proteases on the percentage inhibition of soluble proteases (α = 0.05). Kruskal-Wallis one-way ANOVA and Dunn's multiple comparison tests were used to analyse the effect of PA on loss of dry mass and hydroxyproline content over time (α = 0.05). Results Proanthocyanidin inactivated more than 90% of soluble recombinant MMP-2, -8 and -9 and around 75-90% of cysteine cathepsin B and K, which was significantly higher than CHX (P < 0.05). The inhibition of endogenous proteases by PA increased in a dose-dependent manner. The loss of dry mass and hydroxyproline release in the medium over time was the lowest in dentine beams pretreated with PA < CHX < control (P < 0.05). Conclusion Proanthocyanidin exhibited both dentine MMP and cysteine cathepsins inhibition, which was higher than chlorhexidine.
KW - Collagen cross-linking
KW - Cystein cathepsins
KW - Dentine
KW - Matrix metalloproteinases
KW - Proanthocyanidin
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U2 - 10.1016/j.jdent.2013.06.002
DO - 10.1016/j.jdent.2013.06.002
M3 - Article
C2 - 23806340
AN - SCOPUS:84882456412
SN - 0300-5712
VL - 41
SP - 832
EP - 839
JO - Journal of Dentistry
JF - Journal of Dentistry
IS - 9
ER -