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Zymographic Analysis and Characterization of MMP-2 and -9 Forms in Human Sound Dentin

¹ Department of SAU & FAL, University of Bologna, Italy;
² Institute of Histology and Laboratory Analysis, and
⁴ Institute of Morphological Sciences, University ‘Carlo Bo’ of Urbino, Italy;
³ Department of Oral Biology, School of Dentistry, Medical College of Georgia, Augusta, GA, USA; and
⁵ Unit of Dental Sciences and Biomaterials, Department of Biomedicine, University of Trieste, Via Stuparich, 1, I-34129 Trieste, Italy

^* corresponding author, lbreschi{at}units.it

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 resin-bonded 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.

KEY WORDS: dentin • MMP-2 • MMP-9 • Western blotting • zymography • matrix metalloproteinases • gelatinases