Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1177/0022034517747264 http://hdl.handle.net/11449/176068 |
Resumo: | A chelate-and-rinse extrafibrillar calcium chelation dentin bonding concept has recently been developed and investigated for its effectiveness in improving resin-dentin bonding by bridging the gap between wet and dry dentin bonding. The objective of the present study was to evaluate the gelatinolytic activity of hybrid layers (HLs) created using the chelate-and-rinse bonding technique. Gelatinolytic activity within the HL was examined using in situ zymography and confocal laser-scanning microscopy after 24-h storage or after thermomechanical cycling. Dentin specimens were bonded with Prime&Bond NT (Dentsply Sirona) after conditioning with 15 wt% phosphoric acid for 15 s (control) or 15 wt% polymeric chelators (sodium salt of polyacrylic acid; PAAN) of 2 different molecular weights for 60 s. For each reagent, bonding was performed using dry-bonding and wet-bonding techniques (n = 10). Slices containing the adhesive-dentin interface were covered with fluorescein-conjugated gelatin and examined with a confocal laser-scanning microscope. Fluorescence intensity emitted by the hydrolyzed fluorescein-conjugated gelatin was quantified. Gelatinolytic activity was expressed as the percentage of green fluorescence emitted within the HL. After storage for 24 h, enzymatic activity was only detected within the completely demineralized phosphoric acid–etched dentin, with values derived from dry bonding higher than those from wet bonding (P < 0.05). Almost no fluorescence signals were detected within the HL when dentin was conditioned with PAANs compared with the controls (P < 0.05). After thermomechanical cycling, enzymatic activities significantly increased for the phosphoric acid–conditioned, drying-bonding group compared with 24-h storage (P < 0.05). The present study showed that the use of the chelate-and-rinse bonding concept for both dry-bonding and wet-bonding approaches results in the near absence of matrix-bound collagenolytic activities in the HL even after aging. This may be attributed to fossilization of endogenous proteases via preservation of intrafibrillar minerals within the dentin collagen matrix. |
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Zymography of Hybrid Layers Created Using Extrafibrillar Demineralizationbondingchelationdentinenzymologymatrix metalloproteinasesmicroscopyA chelate-and-rinse extrafibrillar calcium chelation dentin bonding concept has recently been developed and investigated for its effectiveness in improving resin-dentin bonding by bridging the gap between wet and dry dentin bonding. The objective of the present study was to evaluate the gelatinolytic activity of hybrid layers (HLs) created using the chelate-and-rinse bonding technique. Gelatinolytic activity within the HL was examined using in situ zymography and confocal laser-scanning microscopy after 24-h storage or after thermomechanical cycling. Dentin specimens were bonded with Prime&Bond NT (Dentsply Sirona) after conditioning with 15 wt% phosphoric acid for 15 s (control) or 15 wt% polymeric chelators (sodium salt of polyacrylic acid; PAAN) of 2 different molecular weights for 60 s. For each reagent, bonding was performed using dry-bonding and wet-bonding techniques (n = 10). Slices containing the adhesive-dentin interface were covered with fluorescein-conjugated gelatin and examined with a confocal laser-scanning microscope. Fluorescence intensity emitted by the hydrolyzed fluorescein-conjugated gelatin was quantified. Gelatinolytic activity was expressed as the percentage of green fluorescence emitted within the HL. After storage for 24 h, enzymatic activity was only detected within the completely demineralized phosphoric acid–etched dentin, with values derived from dry bonding higher than those from wet bonding (P < 0.05). Almost no fluorescence signals were detected within the HL when dentin was conditioned with PAANs compared with the controls (P < 0.05). After thermomechanical cycling, enzymatic activities significantly increased for the phosphoric acid–conditioned, drying-bonding group compared with 24-h storage (P < 0.05). The present study showed that the use of the chelate-and-rinse bonding concept for both dry-bonding and wet-bonding approaches results in the near absence of matrix-bound collagenolytic activities in the HL even after aging. This may be attributed to fossilization of endogenous proteases via preservation of intrafibrillar minerals within the dentin collagen matrix.Department of Operative Dentistry and Endodontics Guanghua School of Stomatology & Guangdong Provincial Key Laboratory of Stomatology Sun Yat-sen UniversityDepartment of Biomedical and Neuromotor Sciences DIBINEM University of Bologna–Alma Mater StudiorumState Key Laboratory of Oral Diseases West China Hospital of Stomatology Sichuan UniversityDepartment of Restorative Dentistry Institute of Science and Technology São Paulo State University UNESP São Jose dos CamposDepartment of Endodontics The Dental College of Georgia Augusta UniversityState Key Laboratory of Military Stomatology & National Clinical Research Center for Oral Diseases & Shaanxi Key Laboratory of Oral Diseases Department of Prosthodontics School of Stomatology The Fourth Military Medical UniversityDepartment of Restorative Dentistry Institute of Science and Technology São Paulo State University UNESP São Jose dos CamposSun Yat-sen UniversityUniversity of Bologna–Alma Mater StudiorumSichuan UniversityUniversidade Estadual Paulista (Unesp)Augusta UniversityThe Fourth Military Medical UniversityGu, L.Mazzoni, A.Gou, Y.Pucci, C. [UNESP]Breschi, L.Pashley, D. H.Niu, L.Tay, F. R.2018-12-11T17:18:46Z2018-12-11T17:18:46Z2018-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article409-415application/pdfhttp://dx.doi.org/10.1177/0022034517747264Journal of Dental Research, v. 97, n. 4, p. 409-415, 2018.1544-05910022-0345http://hdl.handle.net/11449/17606810.1177/00220345177472642-s2.0-850443934672-s2.0-85044393467.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Dental Research2,302info:eu-repo/semantics/openAccess2023-10-28T06:05:01Zoai:repositorio.unesp.br:11449/176068Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:13:25.292154Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
title |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
spellingShingle |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization Gu, L. bonding chelation dentin enzymology matrix metalloproteinases microscopy |
title_short |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
title_full |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
title_fullStr |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
title_full_unstemmed |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
title_sort |
Zymography of Hybrid Layers Created Using Extrafibrillar Demineralization |
author |
Gu, L. |
author_facet |
Gu, L. Mazzoni, A. Gou, Y. Pucci, C. [UNESP] Breschi, L. Pashley, D. H. Niu, L. Tay, F. R. |
author_role |
author |
author2 |
Mazzoni, A. Gou, Y. Pucci, C. [UNESP] Breschi, L. Pashley, D. H. Niu, L. Tay, F. R. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Sun Yat-sen University University of Bologna–Alma Mater Studiorum Sichuan University Universidade Estadual Paulista (Unesp) Augusta University The Fourth Military Medical University |
dc.contributor.author.fl_str_mv |
Gu, L. Mazzoni, A. Gou, Y. Pucci, C. [UNESP] Breschi, L. Pashley, D. H. Niu, L. Tay, F. R. |
dc.subject.por.fl_str_mv |
bonding chelation dentin enzymology matrix metalloproteinases microscopy |
topic |
bonding chelation dentin enzymology matrix metalloproteinases microscopy |
description |
A chelate-and-rinse extrafibrillar calcium chelation dentin bonding concept has recently been developed and investigated for its effectiveness in improving resin-dentin bonding by bridging the gap between wet and dry dentin bonding. The objective of the present study was to evaluate the gelatinolytic activity of hybrid layers (HLs) created using the chelate-and-rinse bonding technique. Gelatinolytic activity within the HL was examined using in situ zymography and confocal laser-scanning microscopy after 24-h storage or after thermomechanical cycling. Dentin specimens were bonded with Prime&Bond NT (Dentsply Sirona) after conditioning with 15 wt% phosphoric acid for 15 s (control) or 15 wt% polymeric chelators (sodium salt of polyacrylic acid; PAAN) of 2 different molecular weights for 60 s. For each reagent, bonding was performed using dry-bonding and wet-bonding techniques (n = 10). Slices containing the adhesive-dentin interface were covered with fluorescein-conjugated gelatin and examined with a confocal laser-scanning microscope. Fluorescence intensity emitted by the hydrolyzed fluorescein-conjugated gelatin was quantified. Gelatinolytic activity was expressed as the percentage of green fluorescence emitted within the HL. After storage for 24 h, enzymatic activity was only detected within the completely demineralized phosphoric acid–etched dentin, with values derived from dry bonding higher than those from wet bonding (P < 0.05). Almost no fluorescence signals were detected within the HL when dentin was conditioned with PAANs compared with the controls (P < 0.05). After thermomechanical cycling, enzymatic activities significantly increased for the phosphoric acid–conditioned, drying-bonding group compared with 24-h storage (P < 0.05). The present study showed that the use of the chelate-and-rinse bonding concept for both dry-bonding and wet-bonding approaches results in the near absence of matrix-bound collagenolytic activities in the HL even after aging. This may be attributed to fossilization of endogenous proteases via preservation of intrafibrillar minerals within the dentin collagen matrix. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-11T17:18:46Z 2018-12-11T17:18:46Z 2018-04-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1177/0022034517747264 Journal of Dental Research, v. 97, n. 4, p. 409-415, 2018. 1544-0591 0022-0345 http://hdl.handle.net/11449/176068 10.1177/0022034517747264 2-s2.0-85044393467 2-s2.0-85044393467.pdf |
url |
http://dx.doi.org/10.1177/0022034517747264 http://hdl.handle.net/11449/176068 |
identifier_str_mv |
Journal of Dental Research, v. 97, n. 4, p. 409-415, 2018. 1544-0591 0022-0345 10.1177/0022034517747264 2-s2.0-85044393467 2-s2.0-85044393467.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Dental Research 2,302 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
409-415 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128619700027392 |