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Extracellular Signal-Regulated Kinase 1/2 Is Involved in Ascorbic Acid–Induced Osteoblastic Differentiation in Periodontal Ligament Cells

  • Autores: Kaori Mimori
  • Localización: Journal of periodontology, ISSN 0022-3492, Vol. 78, Nº. 2, 2007, págs. 328-334
  • Idioma: inglés
  • Texto completo no disponible (Saber más ...)
  • Resumen
    • Background: Periodontal ligament (PDL) cells possess osteoblast-like properties and play key roles in periodontal regeneration. Previously, we have reported that ascorbic acid promotes the osteoblastic differentiation of PDL cells by modulating the type I collagen–integrin interaction. However, the signaling pathway activated following collagen–integrin interaction is still unclear. In this study, we examined the involvement of extracellular signal-regulated kinase (ERK)1/2 in the expression of osteoblastic marker genes such as the osteoblast-specific transcriptional factor runt-related transcription factor 2 (Runx2), alkaline phosphatase (ALP), and osteocalcin (OCN) in PDL cells.

      Methods: PDL cells were cultured on a conventional or type I collagen–coated dish in the presence or absence of ascorbic acid and examined for ALP activity and osteoblastic marker genes. For detection of ERK1/2, cells were plated on a petri (non-adhesive) dish or type I collagen–coated dish, and Western blot analysis was performed. The effect of the ERK1/2 inhibitor on osteoblastic marker gene expression was examined.

      Results: Ascorbic acid increased gene expression of Runx2, ALP, and OCN. A combination of ascorbic acid and type I collagen remarkably upregulated Runx2, ALP, and OCN gene expression and ALP activity. Western blot analysis revealed an increased level of ERK1/2 phosphorylation in cells plated on type I collagen. An ERK1/2 inhibitor suppressed ascorbic acid–induced ALP and OCN gene expression, whereas Runx2 was not affected in PDL cells.

      Conclusion: These results indicate that ERK1/2 is involved in ascorbic acid–induced osteoblastic differentiation during PDL cell attachment to type I collagen.


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