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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Tezvergil-Mutluay, Arzu
University of Turku
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (10/10 displayed)
- 2021Dry bonding to dentincitations
- 2021The pursuit of resin-dentin bond durabilitycitations
- 2020Incorporation of dimethyl sulfoxide to model adhesive resins with different hydrophilicities : Physico/mechanical propertiescitations
- 2019Incorporation of dimethyl sulfoxide to model adhesive resins with different hydrophilicitiescitations
- 2018Optimization of the etch-and-rinse techniquecitations
- 2018Microtensile bond strength to phosphoric acid-etched dentin treated with NaF, KF and CaF2citations
- 2018Biochemical and immunohistochemical identification of MMP-7 in human dentincitations
- 2016Dentin bond optimization using the dimethyl sulfoxide-wet bonding strategycitations
- 2015Effect of ultraviolet A-induced crosslinking on dentin collagen matrixcitations
- 2013The effect of surface roughness on repair bond strength of light-curing composite resin to polymer composite substrate.citations
Places of action
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article
Biochemical and immunohistochemical identification of MMP-7 in human dentin
Abstract
<p>Objectives: Matrix metalloproteinases (MMPs) are dentinal endogenous enzymes claimed to have a vital role in dentin organic matrix breakdown. The aim of the study was to investigate presence, localization and distribution of MMP-7 in sound human dentin.</p><p>Methods: Dentin was powdered, demineralized and dissolved in isoelectric focusing buffer. Resolved proteins were transferred to nitrocellulose membranes for western blotting (WB) analyses. For the zymographic analysis, aliquots of dentin protein were electrophoresed in 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis containing fluorescently labeled gelatin. Further, the concentrations of dentinal MMPs were measured using Fluorescent Microsphere Immunoassay with a human MMP-MAP multiplex kit. Pre- and post-embedding immunolabeling technique was used to investigate the localization and distribution of MMP-7 in dentin. Dentin was cryo-fractured, the fragments partially decalcified and labeled with a primary monoclonal anti-MMP-7 and a secondary antibody conjugated with gold nanoparticles. MMP-7 labelings were identified in the demineralized dentin matrix as highly electron-dense dispersed gold particles.</p><p>Results: WB and zymographic analysis of extracted dentin proteins showed presence of MMP-7 (similar to 20-28 KDa). Further, MMP-7 was found in the supernatants of the incubated dentin beams using Fluorescent Microsphere Immunoassay. FEI-SEM and TEM analyses established MMP-7 as an intrinsic constituent of the human dentin organic matrix.</p><p>Conclusion: This study demonstrated that MMP-7 is an endogenous component of the human dentin fibrillar network.</p><p>Clinical significance: It is pivotal to understand the underlying processes behind dentin matrix remodeling and degradation in order to develop the most optimal clinical protocols and ensure the longevity of dental restorations.</p>