R Seseogullari-Dirihan1, M M Mutluay2, P Vallittu3, D H Pashley4, A Tezvergil-Mutluay5. 1. Finnish Doctoral Program in Oral Sciences (FINDOS) University of Turku, Institute of Dentistry, Turku, Finland; Adhesive Dentistry Research Group, Institute of Dentistry, University of Turku, Turku, Finland. Electronic address: dirose@utu.fi. 2. Adhesive Dentistry Research Group, Institute of Dentistry, University of Turku, Turku, Finland; Department of Restorative Dentistry and Endodontics, Institute of Dentistry, Turku, Finland. 3. Department of Biomaterials University of Turku, Institute of Dentistry, Turku, Finland. 4. School of Dentistry, Georgia Regents University, Augusta, GA, USA. 5. Adhesive Dentistry Research Group, Institute of Dentistry, University of Turku, Turku, Finland; Department of Restorative Dentistry and Endodontics, Institute of Dentistry, Turku, Finland; Turku University Hospital, TYKS, University of Turku, Turku, Finland.
Abstract
OBJECTIVES: This study evaluated the effect of dentin pretreatment with collagen crosslinkers on matrix metalloproteinase (MMP) and cathepsin K mediated collagen degradation. METHODS: Dentin beams (1mm×2mm×6mm) were demineralized in 10% H3PO4 for 24h. After baseline measurements of dry mass, beams were divided into 11 groups (n=10/group) and, were pretreated for 5min with 1% glutaraldehyde (GA); 5% GA; 1% grape-seed extract (GS); 5% GS; 10% sumac (S); 20μM curcumin (CR); 200μM CR; 0.l% riboflavin/UV (R); 0.5% R; 0.1% riboflavin-5-phosphate/UV (RP); and control (no pretreatment). After pretreatment, the beams were blot-dried and incubated in 1mL calcium and zinc-containing medium (CM, pH 7.2) at 37°C for 3, 7 or 14 days. After incubation, dry mass was reassessed and aliquots of the incubation media were analyzed for collagen C-telopeptides, ICTP and CTX using specific ELISA kits. Data were analyzed by repeated-measures ANOVA. RESULTS: The rate of dry mass loss was significantly different among test groups (p<0.05). The lowest 14 day mean dry mass loss was 6.98%±1.99 in the 200μM curcumin group compared to control loss of dry mass at 32.59%±5.62, p<0.05, at 14 days. The ICTP release over the incubation period (ng/mg dry dentin) ranged between 1.8±0.51 and 31.8±1.8. CTX release from demineralized beams pretreated with crosslinkers was significantly lower than CM (5.7±0.2ng/mg dry dentin). SIGNIFICANCE: The results of this study indicate that collagen crosslinkers tested in this study are good inhibitors of cathepsin K activity in dentin. However, their inhibitory effect on MMP activity was highly variable.
OBJECTIVES: This study evaluated the effect of dentin pretreatment with collagen crosslinkers on matrix metalloproteinase (MMP) and cathepsin K mediated collagen degradation. METHODS: Dentin beams (1mm×2mm×6mm) were demineralized in 10% H3PO4 for 24h. After baseline measurements of dry mass, beams were divided into 11 groups (n=10/group) and, were pretreated for 5min with 1% glutaraldehyde (GA); 5% GA; 1% grape-seed extract (GS); 5% GS; 10% sumac (S); 20μM curcumin (CR); 200μM CR; 0.l% riboflavin/UV (R); 0.5% R; 0.1% riboflavin-5-phosphate/UV (RP); and control (no pretreatment). After pretreatment, the beams were blot-dried and incubated in 1mL calcium and zinc-containing medium (CM, pH 7.2) at 37°C for 3, 7 or 14 days. After incubation, dry mass was reassessed and aliquots of the incubation media were analyzed for collagen C-telopeptides, ICTP and CTX using specific ELISA kits. Data were analyzed by repeated-measures ANOVA. RESULTS: The rate of dry mass loss was significantly different among test groups (p<0.05). The lowest 14 day mean dry mass loss was 6.98%±1.99 in the 200μM curcumin group compared to control loss of dry mass at 32.59%±5.62, p<0.05, at 14 days. The ICTP release over the incubation period (ng/mg dry dentin) ranged between 1.8±0.51 and 31.8±1.8. CTX release from demineralized beams pretreated with crosslinkers was significantly lower than CM (5.7±0.2ng/mg dry dentin). SIGNIFICANCE: The results of this study indicate that collagen crosslinkers tested in this study are good inhibitors of cathepsin K activity in dentin. However, their inhibitory effect on MMP activity was highly variable.
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