TY - JOUR
T1 - Effect of phosphoric acid on the degradation of human dentin matrix
AU - Tezvergil-Mutluay, A.
AU - Mutluay, M.
AU - Seseogullari-Dirihan, R.
AU - Agee, K. A.
AU - Key, W. O.
AU - Scheffel, D. L.S.
AU - Breschi, L.
AU - Mazzoni, A.
AU - Tjäderhane, L.
AU - Nishitani, Y.
AU - Tay, F. R.
AU - Pashley, D. H.
N1 - Funding Information:
This work was supported by grant R01 DE015306 from the National Institute of Dental and Craniofacial Research (P.I. DHP) and by grant #8126372 from the Academy of Finland (P.I. AM).
PY - 2013/1
Y1 - 2013/1
N2 - 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.
AB - 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.
KW - MMPs
KW - bonding
KW - cathepsins
KW - collagen
KW - demineralized
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U2 - 10.1177/0022034512466264
DO - 10.1177/0022034512466264
M3 - Article
C2 - 23103634
AN - SCOPUS:84870925270
SN - 0022-0345
VL - 92
SP - 87
EP - 91
JO - Journal of Dental Research
JF - Journal of Dental Research
IS - 1
ER -