Adenosine monophosphate-activated protein kinase/mammalian target of rapamycin-dependent autophagy protects human dental pulp cells against hypoxia

J Endod. 2013 Jun;39(6):768-73. doi: 10.1016/j.joen.2013.02.001. Epub 2013 Mar 16.

Abstract

Introduction: Human dental pulp cells (HDPCs) are recalcitrant to hypoxic stress. We investigated whether hypoxia-induced autophagy of HDPCs offered these cells a survival advantage and the underlying mechanism of this resistance.

Methods: The viability and apoptosis of HDPCs were examined after exposure to hypoxia by Vi-CELL cell viability analyzer and flow cytometry. Autophagy was assessed by using immunofluorescence, acridine orange staining, real-time polymerase chain reaction, and Western blotting. Either 3-methyladenine or expression vectors encoding dominant negative ATG5 were used to inhibit autophagy. Rapamycin was used as an autophagic inducer. To explore the mechanisms of autophagy, adenosine monophosphate-activated protein kinase (AMPK)/mammalian target of rapamycin (mTOR) pathway and hypoxia-inducible transcription factor-1 were suppressed by chemical inhibitors Compound C and YC-1, respectively.

Results: The exposure of HDPCs to hypoxia had no effect on viability and resulted in increasing acidic vesicular organelle-positive cells, autophagosome formation, and up-regulation of autophagy genes. Inhibition of autophagy with 3- methyladenine or expression vectors encoding dominant negative ATG5 abrogated the protective effects of HDPCs. The phosphorylation of AMPK was up-regulated, whereas the phosphorylation of mTOR was down-regulated in hypoxia-treated HDPCs, which were both attenuated by Compound C. Furthermore, treatment with Compound C rather than YC-1 reduced the autophagy.

Conclusions: Our results suggested that autophagy of HDPCs might be cytoprotective against hypoxic stress via the AMPK/mTOR signaling pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases / antagonists & inhibitors
  • AMP-Activated Protein Kinases / physiology*
  • Adenine / analogs & derivatives
  • Adenine / pharmacology
  • Apoptosis / physiology
  • Apoptosis Regulatory Proteins / analysis
  • Autophagy / drug effects
  • Autophagy / physiology*
  • Autophagy-Related Protein 12
  • Autophagy-Related Protein 5
  • Beclin-1
  • Cell Culture Techniques
  • Cell Hypoxia / physiology*
  • Cell Survival / physiology
  • Cells, Cultured
  • Dental Pulp / cytology
  • Dental Pulp / enzymology*
  • Genetic Vectors / genetics
  • Guanylate Cyclase / pharmacology
  • Humans
  • Hypoxia-Inducible Factor 1 / analysis
  • Hypoxia-Inducible Factor 1 / antagonists & inhibitors
  • Indazoles / pharmacology
  • Membrane Proteins / analysis
  • Microtubule-Associated Proteins / analysis
  • Plasmids / genetics
  • Proto-Oncogene Proteins / analysis
  • Small Ubiquitin-Related Modifier Proteins / analysis
  • TOR Serine-Threonine Kinases / antagonists & inhibitors
  • TOR Serine-Threonine Kinases / physiology*
  • Tumor Suppressor Proteins / analysis

Substances

  • ATG12 protein, human
  • ATG5 protein, human
  • Apoptosis Regulatory Proteins
  • Autophagy-Related Protein 12
  • Autophagy-Related Protein 5
  • BECN1 protein, human
  • BNIP3 protein, human
  • Beclin-1
  • Hypoxia-Inducible Factor 1
  • Indazoles
  • MAP1LC3A protein, human
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Proto-Oncogene Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Tumor Suppressor Proteins
  • 3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole
  • 3-methyladenine
  • MTOR protein, human
  • TOR Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Guanylate Cyclase
  • Adenine