The inhibitory effect of proanthocyanidin on soluble and collagen-bound proteases.

Abstract:

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

journal_name

J Dent

journal_title

Journal of dentistry

authors

Epasinghe DJ,Yiu CK,Burrow MF,Hiraishi N,Tay FR

doi

10.1016/j.jdent.2013.06.002

subject

Has Abstract

pub_date

2013-09-01 00:00:00

pages

832-9

issue

9

eissn

0300-5712

issn

1879-176X

pii

S0300-5712(13)00142-5

journal_volume

41

pub_type

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