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

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http://hdl.handle.net/10138/224109

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Hedenbjork-Lager , A , Hamberg , K , Paakkonen , V , Tjaderhane , L & Ericson , D 2016 , ' Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization ' , Archives of Oral Biology , vol. 68 , pp. 66-72 . https://doi.org/10.1016/j.archoralbio.2016.04.003

Title: Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization
Author: Hedenbjork-Lager, Anders; Hamberg, Kristina; Paakkonen, Virve; Tjaderhane, Leo; Ericson, Dan
Contributor: University of Helsinki, Clinicum
Date: 2016-08
Language: eng
Number of pages: 7
Belongs to series: Archives of Oral Biology
ISSN: 0003-9969
URI: http://hdl.handle.net/10138/224109
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 degrees 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. (C) 2016 Elsevier Ltd. All rights reserved.
Subject: Matrix metalloproteinase
Tooth demineralization
Edetic acid
Acetic acid
Collagen
METALLOPROTEINASES MMPS
BACTERIAL-COLONIZATION
CARIES PROGRESSION
IN-SITU
ACTIVATION
INHIBITORS
PROTEINS
LESIONS
ACID
RATS
313 Dentistry
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