Journal
INTERNATIONAL JOURNAL OF ORAL SCIENCE
Volume 3, Issue 4, Pages 192-199Publisher
NATURE PUBLISHING GROUP
DOI: 10.4248/IJOS11070
Keywords
matrix metalloproteinase-2; human coronal dentin; distribution; gelatinolytic activity
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Funding
- Grants-in-Aid for Scientific Research [23300352] Funding Source: KAKEN
- NIAMS NIH HHS [R21 AR057451] Funding Source: Medline
- NIDCR NIH HHS [R01 DE019527] Funding Source: Medline
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The presence of matrix metalloproteinase-2 (MMP-2) in dentin has been reported, but its distribution and activity level in mature human coronal dentin are not well understood. The purpose of this study was to determine the MMP-2 distribution and relative activity in demineralized dentin. Crowns of twenty eight human molars were sectioned into inner (ID), middle (MD), and outer dentin (OD) regions and demineralized. MMP-2 was extracted with 0.33 mol.L-1 EDTA/2 mol.L-1 guanidine-HCl, pH 7.4, and MMP-2 concentration was estimated with enzyme-linked immunoabsorbant assay (ELISA). Further characterization was accomplished by Western blotting analysis and gelatin zymography. The mean concentrations of MMP-2 per mg dentin protein in the dentin regions were significantly different (P=0.043): 0.9 ng (ID), 0.4 ng (MD), and 2.2 ng (OD), respectively. The pattern of MMP-2 concentration was OD>ID>MD. Western blotting analysis detected similar to 66 and similar to 72 kDa immuno-positive proteins corresponding to pro-and mature MMP-2, respectively, in the ID and MD, and a similar to 66 kDa protein in the OD. Gelatinolytic activity consistent with MMP-2 was detected in all regions. Interestingly, the pattern of levels of Western blot immunodetection and gelatinolytic activity was MD>ID>OD. The concentration of MMP-2 in human coronal dentin was highest in the region of dentin that contains the dentinoenamel junction and least in the middle region of dentin. However, levels of Western blot immunodetection and gelatinolytic activity did not correlate with the estimated regional concentrations of MMP-2, potentially indicating region specific protein interactions.
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