4.5 Article

Determination of Matrix Metalloproteinases in Human Radicular Dentin

Journal

JOURNAL OF ENDODONTICS
Volume 35, Issue 5, Pages 686-689

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.joen.2009.02.003

Keywords

Collagenase; crown; enzymes; gelatinase; human tooth; root

Funding

  1. CAPES [3019/07-1]
  2. CNPq [300615/2007-8, 473164/2007-8]
  3. FAPESP [07/54618-4]
  4. Academy of Finland [111724]
  5. Academy of Finland (AKA) [111724, 111724] Funding Source: Academy of Finland (AKA)

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Matrix metalloproteinases (MMPs) are present in sound coronal dentin and may play a role in collagen network degradation in bonded restorations. We investigated whether these enzymes can also be detected in root dentin. Crown and root sections of human teeth were powderized, and dentin proteins were extracted by using guanidine-HCl and EDTA. Extracts were analyzed by zymography and Western blotting for matrix metalloproteinases detection. Zymography revealed gelatinolytic activities in both crown and root dentin samples, corresponding to MMP-2 and MMP-9. MMP-2 was more evident in demineralized root dentin matrix, whereas MMP-9 was mostly extracted from the mineralized compartment of dentin and presented overall lower levels. Western blot analysis detected MMP-8 equally distributed in crown and root dentin. Because MMPs are also present in radicular dentin, their contribution to the degradation of resin-dentin bonds should be addressed in the development of restorative strategies for the root substrate. (J Endod 2009;35:686-689)

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