2023 Volume 15 Issue 1 Pages 7-13
Nucleotide-binding oligomerization domain 1, which is constitutively expressed in human dental pulp fibroblast-like cells (hDPFs), plays a role in pulpal immune responses by sensing γ-D-glutamyl-meso-diaminopimelic acid (iE-DAP) from bacteria. Matrix metalloproteinase-1 (MMP-1) is an important enzyme that degrades type I collagen, an extracellular matrix component, and is involved in the destruction of dental pulp tissue. In the present study, we investigated the involvement of the ERK1/2 signaling pathway in MMP-1 production by iE-DAP-stimulated hDPFs. iE-DAP was not cytotoxic against hDPFs and did not affect their proliferation. A stimulation with iE-DAP enhanced MMP-1 production and ERK1/2 phosphorylation. The ERK1/2 signaling pathway was involved in the production of MMP-1 by iE-DAP-stimulated hDPFs. These results suggest that the induction of MMP-1 production by iE-DAP-stimulated hDPFs exacerbates pulpitis by promoting the degradation of surrounding collagen.
