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Objective: Matrix metalloproteinases (MMPs) and cysteine cathepsins (CCs) are two distinct enzymatic pathways responsible for the degradation of collagen fibrils in demineralized dentin. NaF and KF have been shown to inhibit salivary MMP-2, -9 and CCs. This study investigated the inhibitory effect of calcium fluoride (CaF 2 ) on the dentin matrix-bound MMPs and CCs., Design: Phosphoric acid (10%)-demineralized dentin beams (1 × 2×6 mm) were incubated at 37 °C in an 1 ml of artificial saliva (AS, control), or AS with 6, 12, 24, 48, 120. 179 and 238 mM F containing CaF 2 (n = 10/group) for 1, 7 and 21 days. All groups were further incubated in AS only for 6 months. Total MMP activity, dry mass loss, CTX and hydroxyproline (HYP) analyses were performed after each incubation. The beams were examined under scanning electron microscopy (SEM). MMP-2 and MMP-9 activities were screened with gelatin zymography. Data were analyzed by using ANOVA and Tukey HSD tests (p = .05)., Results: The total MMP activity was similar for all groups after 21 days and 6 months. After 21 days, the cumulative mass loss and CTX levels were lower compared to control for the CaF 2 ≥48 and CaF 2 ≥120 mM, respectively (p < .05). After 6 months, no significant difference was detected in the dry mass loss and CTX compared to the control (p > .05), whereas HYP level was higher with F 24 and 238 mM groups. CaF 2 -like minerals were observed on the beams under SEM. There was no gelatinase inhibition in zymography., Conclusion: CaF 2 does not prevent the degradation of demineralized dentin matrices due to the catalytic activity of MMPs and CCs., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Matrix metalloproteinases (MMPs) and cysteine cathepsins (CCs) degrade the collagen fibrils of demineralized dentin. Sodium fluoride (NaF) has previously been shown to inhibit recombinant MMP-2 and MMP-9. This study aimed to evaluate the efficacy of NaF on the inhibition of dentin-bound MMPs and CCs. Dentin beams were completely demineralized in 10% phosphoric acid. The baseline total MMP activity and dry masses were measured. Beams were assigned to test groups based on similar MMP activity and dry mass (n = 10/group), and incubated in artificial saliva (control) or artificial saliva with NaF containing 6-238 mM fluoride for 1, 7 and 21 days. The dry mass loss and MMP activities were reassessed at each time point. The proteolytic activity was screened by gelatin zymography. ICTP and CTX released to the incubation medium were analyzed as indices of MMP and cathepsin K activity, respectively. The beams were examined under scanning electron microscopy. All NaF doses reduced the dry mass loss after 21 days (p < 0.05). NaF inhibition of the total MMP activity ranged between 5 and 80%. In gelatin zymography, the bands of MMP-2 and MMP-9 became less prominent with increasing NaF levels. NaF did not decrease the released ICTP (p > 0.05). Less CTX release was detected with F ≥179 mM (p < 0.05). CaF2-like minerals were observed on the beams. High levels of NaF may slow the degradation of the dentin matrix due to the inhibition of cathepsin K. Fluoride does not seem effective in the direct inhibition of proteolysis by dentin matrix-bound MMPs. [ABSTRACT FROM AUTHOR]

Recent studies have reported collagen cross-linking after exposure to riboflavin followed by ultraviolet-A (UVA) exposure. This study is the first to investigate the effect of a riboflavin-containing primer on adhesive interface stability and dentinal matrix metalloproteinase activity. Human dentin was etched with 35% phosphoric acid, treated with 0.1% riboflavin, exposed to UVA for 2 min, and bonded with a two-step etch-and-rinse adhesive. Adhesive was applied to control specimens without riboflavin/UVA. Specimens were subjected to microtensile bond strength tests and pulled to failure after storage for 24 hrs, 6 mos, or 1 yr. Interfacial nanoleakage was evaluated by light and transmission electron microscopy. To investigate dentinal matrix metalloproteinase activity, we performed correlative zymographic assays on protein extracts obtained from phosphoric-acid-etched dentin powder with or without riboflavin/UVA treatment and XP Bond. Ultraviolet-activated riboflavin treatment increased the immediate bond strength to dentin at all aging intervals (p < 0.05 vs. control) and decreased interfacial nanoleakage in aged specimens (1 yr; p < 0.05). Zymograms revealed that riboflavin/UVA pre-treatment inhibited dentinal matrix metalloproteinase activity (especially MMP-9). In conclusion, dentinal collagen cross-linking induced by riboflavin/UVA increased immediate bond strength, stabilized the adhesive interface, and inhibited dentin matrix metalloproteinases, thereby increasing the durability of resin-dentin bonds. [ABSTRACT FROM PUBLISHER]