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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/74242
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dc.contributor.authorTezvergil-Mutluay, A.-
dc.contributor.authorMutluay, M.-
dc.contributor.authorSeseogullari-Dirihan, R.-
dc.contributor.authorAgee, K. A.-
dc.contributor.authorKey, W. O.-
dc.contributor.authorScheffel, D. L S-
dc.contributor.authorBreschi, L.-
dc.contributor.authorMazzoni, A.-
dc.contributor.authorTjäderhane, L.-
dc.contributor.authorNishitani, Y.-
dc.contributor.authorTay, F. R.-
dc.contributor.authorPashley, D. H.-
dc.date.accessioned2014-05-27T11:27:30Z-
dc.date.accessioned2016-10-25T18:41:06Z-
dc.date.available2014-05-27T11:27:30Z-
dc.date.available2016-10-25T18:41:06Z-
dc.date.issued2013-01-01-
dc.identifierhttp://dx.doi.org/10.1177/0022034512466264-
dc.identifier.citationJournal of Dental Research, v. 92, n. 1, p. 87-91, 2013.-
dc.identifier.issn0022-0345-
dc.identifier.issn1544-0591-
dc.identifier.urihttp://hdl.handle.net/11449/74242-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/74242-
dc.description.abstractThis 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.en
dc.format.extent87-91-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectbonding-
dc.subjectcathepsins-
dc.subjectcollagen-
dc.subjectdemineralized-
dc.subjectMMPs-
dc.subject4 aminophenylmercuriacetate-
dc.subject4-aminophenylmercuriacetate-
dc.subjectcathepsin-
dc.subjectcollagen type 1-
dc.subjectcollagen type I trimeric cross linked peptide-
dc.subjectcollagen type I trimeric cross-linked peptide-
dc.subjectcollagenase-
dc.subjectcysteine proteinase inhibitor-
dc.subjectdipeptide-
dc.subjectdrug derivative-
dc.subjectenzyme activator-
dc.subjectenzyme precursor-
dc.subjectilomastat-
dc.subjectleucine-
dc.subjectmatrix metalloproteinase-
dc.subjectmatrix metalloproteinase inhibitor-
dc.subjectn [n (3 carboxyoxirane 2 carbonyl)leucyl]agmatine-
dc.subjectpeptide-
dc.subjectpeptide hydrolase-
dc.subjectphenylmercuric acetate-
dc.subjectphosphoric acid-
dc.subjectthiol reagent-
dc.subjectdentin-
dc.subjectdrug antagonism-
dc.subjectdrug effect-
dc.subjectenzymology-
dc.subjecthuman-
dc.subjectmaterials testing-
dc.subjectprotein denaturation-
dc.subjecttime-
dc.subjectCathepsins-
dc.subjectCollagen Type I-
dc.subjectCollagenases-
dc.subjectCysteine Proteinase Inhibitors-
dc.subjectDentin-
dc.subjectDipeptides-
dc.subjectEnzyme Activators-
dc.subjectEnzyme Precursors-
dc.subjectHumans-
dc.subjectLeucine-
dc.subjectMaterials Testing-
dc.subjectMatrix Metalloproteinase Inhibitors-
dc.subjectMatrix Metalloproteinases-
dc.subjectPeptide Hydrolases-
dc.subjectPeptides-
dc.subjectPhenylmercuric Acetate-
dc.subjectPhosphoric Acids-
dc.subjectProtein Denaturation-
dc.subjectSulfhydryl Reagents-
dc.subjectTime Factors-
dc.titleEffect of phosphoric acid on the degradation of human dentin matrixen
dc.typeoutro-
dc.contributor.institutionUniversity of Turku-
dc.contributor.institutionGeorgia Health Sciences University-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversity of Trieste-
dc.contributor.institutionUniversity of Bologna-
dc.contributor.institutionOulu University Hospital-
dc.contributor.institutionGraduate School of Medicine, Dentistry and Pharmaceutical Sciences-
dc.contributor.institutionUnit of Bologna C/o IOR-
dc.description.affiliationAdhesive Dentistry Research Group Institute of Dentistry University of Turku, Turku-
dc.description.affiliationFinnish Doctoral Program in Oral Sciences (FINDOS) Institute of Dentistry University of Turku, 20520 Turku-
dc.description.affiliationDepartment of Oral Biology College of Dental Medicine Georgia Health Sciences University, Augusta, GA-
dc.description.affiliationDepartment of Orthodontics and Pediatric Dentistry Universidade Estadual Paulista-UNESP Araraquara Dental School, Araraquara, São Paulo-
dc.description.affiliationDepartment of Biomedicine Unit of Dental Sciences and Biomaterials University of Trieste, Trieste-
dc.description.affiliationDepartment of SAUandFAL University of Bologna, Bologna-
dc.description.affiliationInstitute of Dentistry University of Oulu Oulu University Hospital, Oulu-
dc.description.affiliationDepartment of Operative Dentistry Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Kita-ku, Okayama, 700-8525-
dc.description.affiliationDepartment of Endodontics College of Dental Medicine Georgia Health Sciences University, Augusta, GA-
dc.description.affiliationIGM-CNR Unit of Bologna C/o IOR, Bologna-
dc.description.affiliationUnespDepartment of Orthodontics and Pediatric Dentistry Universidade Estadual Paulista-UNESP Araraquara Dental School, Araraquara, São Paulo-
dc.identifier.doi10.1177/0022034512466264-
dc.identifier.wosWOS:000312209700015-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Dental Research-
dc.identifier.scopus2-s2.0-84870925270-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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