Effect of phosphoric acid on the degradation of human dentin matrix
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Data
2013-01-01
Autores
Tezvergil-Mutluay, A.
Mutluay, M.
Seseogullari-Dirihan, R.
Agee, K. A.
Key, W. O.
Scheffel, D. L S [UNESP]
Breschi, L.
Mazzoni, A.
Tjäderhane, L.
Nishitani, Y.
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Resumo
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. © 2013 International & American Associations for Dental Research.
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bonding, cathepsins, collagen, demineralized, MMPs, 4 aminophenylmercuriacetate, 4-aminophenylmercuriacetate, cathepsin, collagen type 1, collagen type I trimeric cross linked peptide, collagen type I trimeric cross-linked peptide, collagenase, cysteine proteinase inhibitor, dipeptide, drug derivative, enzyme activator, enzyme precursor, ilomastat, leucine, matrix metalloproteinase, matrix metalloproteinase inhibitor, n [n (3 carboxyoxirane 2 carbonyl)leucyl]agmatine, peptide, peptide hydrolase, phenylmercuric acetate, phosphoric acid, thiol reagent, dentin, drug antagonism, drug effect, enzymology, human, materials testing, protein denaturation, time, Cathepsins, Collagen Type I, Collagenases, Cysteine Proteinase Inhibitors, Dentin, Dipeptides, Enzyme Activators, Enzyme Precursors, Humans, Leucine, Materials Testing, Matrix Metalloproteinase Inhibitors, Matrix Metalloproteinases, Peptide Hydrolases, Peptides, Phenylmercuric Acetate, Phosphoric Acids, Protein Denaturation, Sulfhydryl Reagents, Time Factors
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Journal of Dental Research, v. 92, n. 1, p. 87-91, 2013.