TY - JOUR
T1 - The inhibitory effects of quaternary ammonium methacrylates on soluble and matrix-bound MMPs
AU - Tezvergil-Mutluay, A.
AU - Agee, K. A.
AU - Uchiyama, T.
AU - Imazato, S.
AU - Mutluay, M. M.
AU - Cadenaro, M.
AU - Breschi, L.
AU - Nishitani, Y.
AU - Tay, F. R.
AU - Pashley, D. H.
N1 - Funding Information:
The authors are grateful to Kuraray Medical Inc. for their generous donation of MDPB. This work was supported by R01 DE015306-06 from the National Institute of Dental and Craniofacial Research (NIDCR) to DHP (PI) and by grant #8126472 from the Academy of Finland to AT-M (PI). The authors thank Mrs. Michelle Barnes for her secretarial support.
PY - 2011/4
Y1 - 2011/4
N2 - Matrix metalloproteinases (MMPs) bound to dentin contribute to the progressive degradation of collagen fibrils in hybrid layers created by dentin adhesives. This study evaluated the MMP-inhibiting potential of quaternary ammonium methacrylates (QAMs), with soluble rhMMP-9 and a matrix-bound endogenous MMP model. Six different QAMs were initially screened by a rhMMP-9 colorimetric assay. For the matrix-bound endogenous MMPs, we aged demineralized dentin beams for 30 days in calcium- and zinc-containing media (CM; control), chlorhexidine, or QAMs in CM to determine the changes in dry mass loss and solubilization of collagen peptides against baseline levels. The inhibitory effects of QAMs on soluble rhMMP-9 varied between 34 and 100%. Beams incubated in CM showed a 29% decrease in dry mass (p < 0.05), whereas beams incubated with QAMs showed only 0.2%-6% loss of dry mass. Significantly more solubilized collagen was detected from beams incubated in CM (p < 0.05). It is concluded that QAMs exhibited dentin MMP inhibition comparable with that of chlorhexidine, but required higher concentrations.
AB - Matrix metalloproteinases (MMPs) bound to dentin contribute to the progressive degradation of collagen fibrils in hybrid layers created by dentin adhesives. This study evaluated the MMP-inhibiting potential of quaternary ammonium methacrylates (QAMs), with soluble rhMMP-9 and a matrix-bound endogenous MMP model. Six different QAMs were initially screened by a rhMMP-9 colorimetric assay. For the matrix-bound endogenous MMPs, we aged demineralized dentin beams for 30 days in calcium- and zinc-containing media (CM; control), chlorhexidine, or QAMs in CM to determine the changes in dry mass loss and solubilization of collagen peptides against baseline levels. The inhibitory effects of QAMs on soluble rhMMP-9 varied between 34 and 100%. Beams incubated in CM showed a 29% decrease in dry mass (p < 0.05), whereas beams incubated with QAMs showed only 0.2%-6% loss of dry mass. Significantly more solubilized collagen was detected from beams incubated in CM (p < 0.05). It is concluded that QAMs exhibited dentin MMP inhibition comparable with that of chlorhexidine, but required higher concentrations.
KW - MDPB
KW - dentin
KW - hydroxyproline
KW - matrix metalloproteinase
KW - quaternary ammonium methacrylates
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U2 - 10.1177/0022034510389472
DO - 10.1177/0022034510389472
M3 - Article
C2 - 21212315
AN - SCOPUS:79954584526
SN - 0022-0345
VL - 90
SP - 535
EP - 540
JO - Journal of Dental Research
JF - Journal of Dental Research
IS - 4
ER -