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.Tay, F. R.Pashley, D. H.2014-05-272014-05-272013-01-01Journal of Dental Research, v. 92, n. 1, p. 87-91, 2013.0022-03451544-0591http://hdl.handle.net/11449/74242This 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.87-91engbondingcathepsinscollagendemineralizedMMPs4 aminophenylmercuriacetate4-aminophenylmercuriacetatecathepsincollagen type 1collagen type I trimeric cross linked peptidecollagen type I trimeric cross-linked peptidecollagenasecysteine proteinase inhibitordipeptidedrug derivativeenzyme activatorenzyme precursorilomastatleucinematrix metalloproteinasematrix metalloproteinase inhibitorn [n (3 carboxyoxirane 2 carbonyl)leucyl]agmatinepeptidepeptide hydrolasephenylmercuric acetatephosphoric acidthiol reagentdentindrug antagonismdrug effectenzymologyhumanmaterials testingprotein denaturationtimeCathepsinsCollagen Type ICollagenasesCysteine Proteinase InhibitorsDentinDipeptidesEnzyme ActivatorsEnzyme PrecursorsHumansLeucineMaterials TestingMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesPeptide HydrolasesPeptidesPhenylmercuric AcetatePhosphoric AcidsProtein DenaturationSulfhydryl ReagentsTime FactorsArtigo10.1177/0022034512466264WOS:000312209700015Acesso restrito2-s2.0-84870925270