A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Effect of Phosphoric Acid on the Degradation of Human Dentin Matrix
Tekijät: Tezvergil-Mutluay A, Mutluay M, Seseogullari-Dirihan R, Agee KA, Key WO, Scheffel DLS, Breschi L, Mazzoni A, Tjaderhane L, Nishitani Y, Tay FR, Pashley DH
Kustantaja: SAGE PUBLICATIONS INC
Julkaisuvuosi: 2013
Lehti: Journal of Dental Research
Tietokannassa oleva lehden nimi: JOURNAL OF DENTAL RESEARCH
Lehden akronyymi: J DENT RES
Numero sarjassa: 1
Vuosikerta: 92
Numero: 1
Aloitussivu: 87
Lopetussivu: 91
Sivujen määrä: 5
ISSN: 0022-0345
DOI: https://doi.org/10.1177/0022034512466264
Tiivistelmä
This study determined if dentin proteases are denatured by phosphoric acid (PA) used in etch-and-rinse dentin adhesives. Dentin beams were completely demineralized with EDTA for 30 days. We "acid-etched" experimental groups by exposing the demineralized dentin beams to 1, 10, or 37 mass% PA for 15 sec or 15 min. Control beams were not exposed to PA but were incubated in simulated body fluid for 3 days to assay their total endogenous telopeptidase activity, by their ability to solubilize C-terminal crosslinked telopeptides ICTP and CTX from insoluble dentin collagen. Control beams released 6.1 +/- 0.8 ng ICTP and 0.6 +/- 0.1 ng CTX/mg dry-wt/3 days. Positive control beams pre-incubated in p-aminophenylmercuric acetate, a compound known to activate proMMPs, released about the same amount of ICTP peptides, but released significantly less CTX. Beams immersed in 1, 10, or 37 mass% PA for 15 sec or 15 min released amounts of ICTP and CTX similar to that released by the controls (p > 0.05). Beams incubated in galardin, an MMP inhibitor, or E-64, a cathepsin inhibitor, blocked most of the release of ICTP and CTX, respectively. It is concluded that PA does not denature endogenous MMP and cathepsin activities of dentin matrices.
This study determined if dentin proteases are denatured by phosphoric acid (PA) used in etch-and-rinse dentin adhesives. Dentin beams were completely demineralized with EDTA for 30 days. We "acid-etched" experimental groups by exposing the demineralized dentin beams to 1, 10, or 37 mass% PA for 15 sec or 15 min. Control beams were not exposed to PA but were incubated in simulated body fluid for 3 days to assay their total endogenous telopeptidase activity, by their ability to solubilize C-terminal crosslinked telopeptides ICTP and CTX from insoluble dentin collagen. Control beams released 6.1 +/- 0.8 ng ICTP and 0.6 +/- 0.1 ng CTX/mg dry-wt/3 days. Positive control beams pre-incubated in p-aminophenylmercuric acetate, a compound known to activate proMMPs, released about the same amount of ICTP peptides, but released significantly less CTX. Beams immersed in 1, 10, or 37 mass% PA for 15 sec or 15 min released amounts of ICTP and CTX similar to that released by the controls (p > 0.05). Beams incubated in galardin, an MMP inhibitor, or E-64, a cathepsin inhibitor, blocked most of the release of ICTP and CTX, respectively. It is concluded that PA does not denature endogenous MMP and cathepsin activities of dentin matrices.
Avainsanat:
bonding, cathepsins, collagen, demineralized, MMPs
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