Biomechanical force induces the growth factor production in human periodontal ligament-derived cells

Odontology. 2016 Jan;104(1):27-34. doi: 10.1007/s10266-015-0206-5. Epub 2015 May 10.

Abstract

Although many reports have been published on the functional roles of periodontal ligament (PDL) cells, the mechanisms involved in the maintenance and homeostasis of PDL have not been determined. We investigated the effects of biomechanical force on growth factor production, phosphorylation of MAPKs, and intracellular transduction pathways for growth factor production in human periodontal ligament (hPDL) cells using MAPK inhibitors. hPDL cells were exposed to mechanical force (6 MPa) using a hydrostatic pressure apparatus. The levels of growth factor mRNA and protein were examined by real-time RT-PCR and ELISA. The phosphorylation of MAPKs was measured using BD™ CBA Flex Set. In addition, MAPKs inhibitors were used to identify specific signal transduction pathways. Application of biomechanical force (equivalent to occlusal force) increased the synthesis of VEGF-A, FGF-2, and NGF. The application of biomechanical force increased the expression levels of phosphorylated ERK and p38, but not of JNK. Furthermore, the levels of VEGF-A and NGF expression were suppressed by ERK or p38 inhibitor. The growth factors induced by biomechanical force may play a role in the mechanisms of homeostasis of PDL.

Keywords: Biomechanical force; Growth factor; MAPK; Occlusal force; Periodontal ligament (PDL).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomechanical Phenomena
  • Cell Survival
  • Cells, Cultured
  • Enzyme-Linked Immunosorbent Assay
  • Fibroblast Growth Factor 2 / metabolism*
  • Humans
  • Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinases / metabolism*
  • Nerve Growth Factor / metabolism*
  • Periodontal Ligament / cytology*
  • Phosphorylation
  • Pressure
  • Real-Time Polymerase Chain Reaction
  • Signal Transduction
  • Stress, Mechanical*
  • Vascular Endothelial Growth Factor A / metabolism*

Substances

  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Fibroblast Growth Factor 2
  • Nerve Growth Factor
  • Mitogen-Activated Protein Kinases