SynopsisNucleotide-binding oligomerization domain 2 (NOD2), which is constitutively expressed in human pulp fibroblasts, plays a role in pulpal immune responses by sensing muramyl dipeptide (MDP) from bacteria, which leads to pulpitis. Matrix metalloproteinase-3 (MMP-3), which exhibits broad substrate specificity to the extracellular matrix (ECM) and induces angiogenesis and fibroblast wound healing, is expressed when pulp is inflamed. In the present study, we examined MDP/NOD2-induced MMP-3 production and the role of its signaling cascade involving TAK1/MAP kinase in human deciduous dental pulp fibroblast-like cells (hDDPFs). MDP did not affect the proliferation or viability of hDDPFs. The MAP kinase signaling pathway was involved in the production of MMP-3 in MDP-stimulated hDDPFs. The MDP stimulation enhanced ERK 1/2 phosphorylation, but did not affect the degradation of IκB. These results suggest that the production of MMP-3 in MDP-stimulated hDDPFs stimulated the degradation of surrounding collagen, leading to alterations in the structure of the ECM and inflammation, and appeared to promote angiogenesis.
Key words: NOD2/MDP, MMP-3, MAP kinase, human deciduous dental pulp fibroblast-like cells
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J-Stage
https://www.jstage.jst.go.jp/article/nano/13/2/13_13_41/_article
DOI
https://doi.org/10.11344/nano.13.41