Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization

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Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization

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Publication Article, peer reviewed scientific
Title Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization
Author Hedenbjörk-Lager, Anders ; Hamberg, Kristina ; Pääkkönen, Virve ; Tjäderhane, Leo ; Ericson, Dan
Date 2016
English abstract
OBJECTIVE: Dental caries is a process driven by acids produced by oral microorganisms followed by degradation of the dentine collagen matrix by proteolytic enzymes. Matrix metalloproteinases (MMPs) have been suggested to contribute to caries by degrading collagen. The aim of this study was to develop a method for generating demineralized dentine matrix substrate (DDM) maintaining MMP-8 bioactivity and no interference with later assays. Such a substrate would allow study of the effects of various treatments on MMP-8 activity and collagen degradation in demineralized dentine. DESIGN: Human dentine was powderized in a tissue grinder and frozen (-80°C). The powder was demineralized in dialysis tubes, using EDTA or acetic acid. The demineralized dentine matrix (DDM) was harvested and analyzed for collagen content using SDS-PAGE. The DDM was subsequently suspended in PBS or TESCA buffer. Protein, MMP-8 (ELISA) and collagen (HYP) was analyzed directly or after 1 wk. RESULTS: EDTA or acid demineralization of dentine using dialysis yielded a substrate rich in collagen coupled with preserved MMP-8 activity. Collagen degraded in room temperature, assessed by higher HYP amounts in the soluble fraction of DDM after one wk, indicating that the methods used preserved active DDM-components after the demineralization process. CONCLUSIONS: The presented demineralization methods both provided insoluble DDM substrates suitable for further intervention studies. However, it was found that the substrates differed depending on the demineralization method and buffers used. This needs further study to find an optimal technique for generating DDM with retained proteins as well as enzymatic bioactivity.
DOI https://doi.org/10.1016/j.archoralbio.2016.04.003 (link to publisher's fulltext.)
Publisher Elsevier
Host/Issue Archives of Oral Biology;
Volume 68
ISSN 0003-9969
Pages 66-72
Language eng (iso)
Subject Acetic acid
Collagen
Edetic acid
Matrix metalloproteinase
Tooth demineralization
Medicine
Research Subject Categories::MEDICINE
Handle http://hdl.handle.net/2043/21847 Permalink to this page
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