Zymographic analysis and characterization of MMP-2 and -9 forms in human sound dentin

A. Mazzoni, F. Mannello, F. R. Tay, G. A.M. Tonti, S. Papa, G. Mazzotti, R. Di Lenarda, D. H. Pashley, L. Breschi

Research output: Contribution to journalArticlepeer-review

232 Scopus citations


The role and function of dentin matrix metalloproteinases (MMPs) are not well-understood, but they may play a key role in dentinal caries and the degradation of resinbonded dentin matrices. To test the null hypothesis that MMP-9 is not found in dentin matrix, we used gelatin zymography to extract and isolate all molecular forms of gelatinolytic MMPs in demineralized mature sound dentin powder obtained from extracted human molars, characterizing and identifying the enzymes by Western blotting. Gelatinolytic MMPs were detected in extracts of demineralized dentin matrix and identified as MMP-2 and MMP-9. Acidic extracts (pH 2.3) yielded 3-8 times more MMP activity than did EDTA (pH 7.4). Their activation may contribute to dentin matrix degradation, which occurs during caries progression and following resin bonding. Inhibition of MMP-2 and -9 proteolytic activity may slow caries progression and increase the durability of resin-dentin bonds.

Original languageEnglish (US)
Pages (from-to)436-440
Number of pages5
JournalJournal of Dental Research
Issue number5
StatePublished - May 2007
Externally publishedYes


  • Dentin
  • Gelatinases
  • MMP-2
  • MMP-9
  • Matrix metalloproteinases
  • Western blotting
  • Zymography

ASJC Scopus subject areas

  • Dentistry(all)


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