Stabilization of dentin matrix after cross-linking treatments, in vitro

Débora L.S. Scheffel, Josimeri Hebling, Régis H. Scheffel, Kelli A. Agee, Milena Cadenaro, Gianluca Turco, Lorenzo Breschi, Annalisa Mazzoni, Carlos A. De Souza Costa, David Henry Pashley

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Objectives To evaluate the effect of EDC on elastic modulus (E), MMPs activity, hydroxyproline (HYP) release and thermal denaturation temperature of demineralized dentin collagen. Methods Dentin beams were obtained from human molars and completely demineralized in 10 wt% H3PO4 for 18 h. The initial E and MMP activity were determined with three-point bending and microcolorimetric assay, respectively. Extra demineralized beams were dehydrated and the initial dry mass (DM) was determined. All the beams were distributed into groups (n = 10) and treated for 30 s or 60 s with: water, 0.5 M, 1 M or 2 M EDC or 10% glutaraldehyde (GA). After treatment, the new E and MMP activity were redetermined. The beams submitted to DM measurements were storage for 1 week in artificial saliva, after that the mass loss and HYP release were evaluated. The collagen thermal denaturation temperature (TDT) was determined by DSC analysis. Data for E, MMP activity and HYP release were submitted to Wilcoxon and Kruskal-Wallis or Mann-Whitney tests. Mass loss and TDT data were submitted to ANOVA and Tukey tests at the 5% of significance. Results EDC was able to significantly increase collagen stiffness in 60 s. 10% GA groups obtained the highest E values after both 30 and 60 s. All cross-linking agents decreased MMP activity and HYP release and increased TDT temperature. Significant differences were identified among EDC groups after 30 or 60 s of cross-linking, 1 M or 2 M EDC showed the lowest MMP activity. Significance Cross-linking agents are capable of preventing dentin collagen degradation. EDC treatment may be clinically useful to increase resin-dentin stability.

Original languageEnglish (US)
Pages (from-to)227-233
Number of pages7
JournalDental Materials
Volume30
Issue number2
DOIs
StatePublished - Feb 1 2014

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Hydroxyproline
Dentin
Matrix Metalloproteinases
Denaturation
Collagen
Stabilization
Hot Temperature
Temperature
Glutaral
Artificial Saliva
Analysis of variance (ANOVA)
Elastic Modulus
Assays
Thermodynamic properties
Resins
Elastic moduli
Stiffness
In Vitro Techniques
Analysis of Variance
Degradation

Keywords

  • Collagen
  • Cross-linkers
  • Dentin
  • EDC
  • Glutaraldehyde
  • MMPs

ASJC Scopus subject areas

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

Cite this

Scheffel, D. L. S., Hebling, J., Scheffel, R. H., Agee, K. A., Cadenaro, M., Turco, G., ... Pashley, D. H. (2014). Stabilization of dentin matrix after cross-linking treatments, in vitro. Dental Materials, 30(2), 227-233. https://doi.org/10.1016/j.dental.2013.11.007

Stabilization of dentin matrix after cross-linking treatments, in vitro. / Scheffel, Débora L.S.; Hebling, Josimeri; Scheffel, Régis H.; Agee, Kelli A.; Cadenaro, Milena; Turco, Gianluca; Breschi, Lorenzo; Mazzoni, Annalisa; De Souza Costa, Carlos A.; Pashley, David Henry.

In: Dental Materials, Vol. 30, No. 2, 01.02.2014, p. 227-233.

Research output: Contribution to journalArticle

Scheffel, DLS, Hebling, J, Scheffel, RH, Agee, KA, Cadenaro, M, Turco, G, Breschi, L, Mazzoni, A, De Souza Costa, CA & Pashley, DH 2014, 'Stabilization of dentin matrix after cross-linking treatments, in vitro', Dental Materials, vol. 30, no. 2, pp. 227-233. https://doi.org/10.1016/j.dental.2013.11.007
Scheffel DLS, Hebling J, Scheffel RH, Agee KA, Cadenaro M, Turco G et al. Stabilization of dentin matrix after cross-linking treatments, in vitro. Dental Materials. 2014 Feb 1;30(2):227-233. https://doi.org/10.1016/j.dental.2013.11.007
Scheffel, Débora L.S. ; Hebling, Josimeri ; Scheffel, Régis H. ; Agee, Kelli A. ; Cadenaro, Milena ; Turco, Gianluca ; Breschi, Lorenzo ; Mazzoni, Annalisa ; De Souza Costa, Carlos A. ; Pashley, David Henry. / Stabilization of dentin matrix after cross-linking treatments, in vitro. In: Dental Materials. 2014 ; Vol. 30, No. 2. pp. 227-233.
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abstract = "Objectives To evaluate the effect of EDC on elastic modulus (E), MMPs activity, hydroxyproline (HYP) release and thermal denaturation temperature of demineralized dentin collagen. Methods Dentin beams were obtained from human molars and completely demineralized in 10 wt{\%} H3PO4 for 18 h. The initial E and MMP activity were determined with three-point bending and microcolorimetric assay, respectively. Extra demineralized beams were dehydrated and the initial dry mass (DM) was determined. All the beams were distributed into groups (n = 10) and treated for 30 s or 60 s with: water, 0.5 M, 1 M or 2 M EDC or 10{\%} glutaraldehyde (GA). After treatment, the new E and MMP activity were redetermined. The beams submitted to DM measurements were storage for 1 week in artificial saliva, after that the mass loss and HYP release were evaluated. The collagen thermal denaturation temperature (TDT) was determined by DSC analysis. Data for E, MMP activity and HYP release were submitted to Wilcoxon and Kruskal-Wallis or Mann-Whitney tests. Mass loss and TDT data were submitted to ANOVA and Tukey tests at the 5{\%} of significance. Results EDC was able to significantly increase collagen stiffness in 60 s. 10{\%} GA groups obtained the highest E values after both 30 and 60 s. All cross-linking agents decreased MMP activity and HYP release and increased TDT temperature. Significant differences were identified among EDC groups after 30 or 60 s of cross-linking, 1 M or 2 M EDC showed the lowest MMP activity. Significance Cross-linking agents are capable of preventing dentin collagen degradation. EDC treatment may be clinically useful to increase resin-dentin stability.",
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AU - Scheffel, Débora L.S.

AU - Hebling, Josimeri

AU - Scheffel, Régis H.

AU - Agee, Kelli A.

AU - Cadenaro, Milena

AU - Turco, Gianluca

AU - Breschi, Lorenzo

AU - Mazzoni, Annalisa

AU - De Souza Costa, Carlos A.

AU - Pashley, David Henry

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N2 - Objectives To evaluate the effect of EDC on elastic modulus (E), MMPs activity, hydroxyproline (HYP) release and thermal denaturation temperature of demineralized dentin collagen. Methods Dentin beams were obtained from human molars and completely demineralized in 10 wt% H3PO4 for 18 h. The initial E and MMP activity were determined with three-point bending and microcolorimetric assay, respectively. Extra demineralized beams were dehydrated and the initial dry mass (DM) was determined. All the beams were distributed into groups (n = 10) and treated for 30 s or 60 s with: water, 0.5 M, 1 M or 2 M EDC or 10% glutaraldehyde (GA). After treatment, the new E and MMP activity were redetermined. The beams submitted to DM measurements were storage for 1 week in artificial saliva, after that the mass loss and HYP release were evaluated. The collagen thermal denaturation temperature (TDT) was determined by DSC analysis. Data for E, MMP activity and HYP release were submitted to Wilcoxon and Kruskal-Wallis or Mann-Whitney tests. Mass loss and TDT data were submitted to ANOVA and Tukey tests at the 5% of significance. Results EDC was able to significantly increase collagen stiffness in 60 s. 10% GA groups obtained the highest E values after both 30 and 60 s. All cross-linking agents decreased MMP activity and HYP release and increased TDT temperature. Significant differences were identified among EDC groups after 30 or 60 s of cross-linking, 1 M or 2 M EDC showed the lowest MMP activity. Significance Cross-linking agents are capable of preventing dentin collagen degradation. EDC treatment may be clinically useful to increase resin-dentin stability.

AB - Objectives To evaluate the effect of EDC on elastic modulus (E), MMPs activity, hydroxyproline (HYP) release and thermal denaturation temperature of demineralized dentin collagen. Methods Dentin beams were obtained from human molars and completely demineralized in 10 wt% H3PO4 for 18 h. The initial E and MMP activity were determined with three-point bending and microcolorimetric assay, respectively. Extra demineralized beams were dehydrated and the initial dry mass (DM) was determined. All the beams were distributed into groups (n = 10) and treated for 30 s or 60 s with: water, 0.5 M, 1 M or 2 M EDC or 10% glutaraldehyde (GA). After treatment, the new E and MMP activity were redetermined. The beams submitted to DM measurements were storage for 1 week in artificial saliva, after that the mass loss and HYP release were evaluated. The collagen thermal denaturation temperature (TDT) was determined by DSC analysis. Data for E, MMP activity and HYP release were submitted to Wilcoxon and Kruskal-Wallis or Mann-Whitney tests. Mass loss and TDT data were submitted to ANOVA and Tukey tests at the 5% of significance. Results EDC was able to significantly increase collagen stiffness in 60 s. 10% GA groups obtained the highest E values after both 30 and 60 s. All cross-linking agents decreased MMP activity and HYP release and increased TDT temperature. Significant differences were identified among EDC groups after 30 or 60 s of cross-linking, 1 M or 2 M EDC showed the lowest MMP activity. Significance Cross-linking agents are capable of preventing dentin collagen degradation. EDC treatment may be clinically useful to increase resin-dentin stability.

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KW - Cross-linkers

KW - Dentin

KW - EDC

KW - Glutaraldehyde

KW - MMPs

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