Effect of pretreatment with collagen crosslinkers on dentin protease activity

R. Seseogullari-Dirihan, M. M. Mutluay, P. Vallittu, David Henry Pashley, A. Tezvergil-Mutluay

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 (1 mm × 2 mm × 6 mm) were demineralized in 10% H3PO4 for 24 h. After baseline measurements of dry mass, beams were divided into 11 groups (n = 10/group) and, were pretreated for 5 min with 1% glutaraldehyde (GA); 5% GA; 1% grape-seed extract (GS); 5% GS; 10% sumac (S); 20 μM curcumin (CR); 200 μM 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 1 mL 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 200 μM 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 ± 0.2 ng/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.

Original languageEnglish (US)
Pages (from-to)941-947
Number of pages7
JournalDental Materials
Volume31
Issue number8
DOIs
StatePublished - Aug 1 2015

Fingerprint

Dentin
Collagen
Curcumin
Peptide Hydrolases
Grape Seed Extract
Cathepsin K
Glutaral
Matrix Metalloproteinases
Seed
Flavin Mononucleotide
Rhus
Riboflavin
Analysis of variance (ANOVA)
Zinc
Calcium
Phosphates
Analysis of Variance
Degradation
Enzyme-Linked Immunosorbent Assay
Cathepsins

Keywords

  • Collagen crosslinker
  • Cysteine cathepsins
  • Dentin
  • Gluteraldehyde
  • Matrix metalloproteinase

ASJC Scopus subject areas

  • Materials Science(all)
  • Dentistry(all)
  • Mechanics of Materials

Cite this

Seseogullari-Dirihan, R., Mutluay, M. M., Vallittu, P., Pashley, D. H., & Tezvergil-Mutluay, A. (2015). Effect of pretreatment with collagen crosslinkers on dentin protease activity. Dental Materials, 31(8), 941-947. https://doi.org/10.1016/j.dental.2015.05.002

Effect of pretreatment with collagen crosslinkers on dentin protease activity. / Seseogullari-Dirihan, R.; Mutluay, M. M.; Vallittu, P.; Pashley, David Henry; Tezvergil-Mutluay, A.

In: Dental Materials, Vol. 31, No. 8, 01.08.2015, p. 941-947.

Research output: Contribution to journalArticle

Seseogullari-Dirihan, R, Mutluay, MM, Vallittu, P, Pashley, DH & Tezvergil-Mutluay, A 2015, 'Effect of pretreatment with collagen crosslinkers on dentin protease activity', Dental Materials, vol. 31, no. 8, pp. 941-947. https://doi.org/10.1016/j.dental.2015.05.002
Seseogullari-Dirihan R, Mutluay MM, Vallittu P, Pashley DH, Tezvergil-Mutluay A. Effect of pretreatment with collagen crosslinkers on dentin protease activity. Dental Materials. 2015 Aug 1;31(8):941-947. https://doi.org/10.1016/j.dental.2015.05.002
Seseogullari-Dirihan, R. ; Mutluay, M. M. ; Vallittu, P. ; Pashley, David Henry ; Tezvergil-Mutluay, A. / Effect of pretreatment with collagen crosslinkers on dentin protease activity. In: Dental Materials. 2015 ; Vol. 31, No. 8. pp. 941-947.
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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 (1 mm × 2 mm × 6 mm) were demineralized in 10{\%} H3PO4 for 24 h. After baseline measurements of dry mass, beams were divided into 11 groups (n = 10/group) and, were pretreated for 5 min with 1{\%} glutaraldehyde (GA); 5{\%} GA; 1{\%} grape-seed extract (GS); 5{\%} GS; 10{\%} sumac (S); 20 μM curcumin (CR); 200 μM 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 1 mL 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 200 μM 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 ± 0.2 ng/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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AU - Vallittu, P.

AU - Pashley, David Henry

AU - Tezvergil-Mutluay, A.

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N2 - 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 (1 mm × 2 mm × 6 mm) were demineralized in 10% H3PO4 for 24 h. After baseline measurements of dry mass, beams were divided into 11 groups (n = 10/group) and, were pretreated for 5 min with 1% glutaraldehyde (GA); 5% GA; 1% grape-seed extract (GS); 5% GS; 10% sumac (S); 20 μM curcumin (CR); 200 μM 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 1 mL 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 200 μM 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 ± 0.2 ng/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.

AB - 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 (1 mm × 2 mm × 6 mm) were demineralized in 10% H3PO4 for 24 h. After baseline measurements of dry mass, beams were divided into 11 groups (n = 10/group) and, were pretreated for 5 min with 1% glutaraldehyde (GA); 5% GA; 1% grape-seed extract (GS); 5% GS; 10% sumac (S); 20 μM curcumin (CR); 200 μM 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 1 mL 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 200 μM 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 ± 0.2 ng/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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KW - Cysteine cathepsins

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KW - Gluteraldehyde

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