Host-derived loss of dentin matrix stiffness associated with solubilization of collagen

Marcela R. Carrilho, Franklin R. Tay, Adam M. Donnelly, Kelli A. Agee, Leo Tjäderhane, Annalisa Mazzoni, Lorenzo Breschi, Stephen Foulger, David H. Pashley

Research output: Contribution to journalArticle

114 Scopus citations

Abstract

Matrix metalloproteinases (MMPs) bound to dentin matrices are activated during adhesive bonding procedures and are thought to contribute to the progressive degradation of resin-dentin bonds over time. The purpose of this study was to evaluate the changes in mechanical, biochemical, and structural properties of demineralized dentin treated with or without chlorhexidine (CHX), a known MMP-inhibitor. After demineralizing dentin beams in EDTA or phosphoric acid (PA), the baseline modulus of elasticity (E) of each beam was measured by three-point flexure. Specimens were pretreated with water (control) or with 2% CHX (experimental) and then incubated in artificial saliva (AS) at 37°C for 4 weeks. The E of each specimen was remeasured weekly and, the media was analyzed for solubilized dentin collagen at first and fourth week of incubation. Some specimens were processed for electron microscopy (TEM) immediately after demineralization and after 4 weeks of incubation. In EDTA and PA-demineralized specimens, the E of the control specimens fell (p < 0.05) after incubation in AS, whereas there were no changes in E of the CHX-pretreated specimens over time. More collagen was solubilized from PA-demineralized controls (p < 0.05) than from EDTA-demineralized matrices after 1 or 4 weeks. Less collagen (p < 0.05) was solubilized from CHX-pretreated specimens demineralized in EDTA compared with PA. TEM examination of control beams revealed that prolonged demineralization of dentin in 10% PA (12 h) did not denature the collagen fibrils.

Original languageEnglish (US)
Pages (from-to)373-380
Number of pages8
JournalJournal of Biomedical Materials Research - Part B Applied Biomaterials
Volume90 B
Issue number1
DOIs
StatePublished - Jul 2009

Keywords

  • Dentin collagen
  • Electron microscopy
  • Matrix metalloproteinase
  • Mechanical properties

ASJC Scopus subject areas

  • Biomaterials
  • Biomedical Engineering

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    Carrilho, M. R., Tay, F. R., Donnelly, A. M., Agee, K. A., Tjäderhane, L., Mazzoni, A., Breschi, L., Foulger, S., & Pashley, D. H. (2009). Host-derived loss of dentin matrix stiffness associated with solubilization of collagen. Journal of Biomedical Materials Research - Part B Applied Biomaterials, 90 B(1), 373-380. https://doi.org/10.1002/jbm.b.31295