Bleomycin induces alveolar epithelial cell death through JNK-dependent activation of the mitochondrial death pathway

Am J Physiol Lung Cell Mol Physiol. 2005 Oct;289(4):L521-8. doi: 10.1152/ajplung.00340.2004.

Abstract

Exposure to bleomycin in rodents induces lung injury and fibrosis. Alveolar epithelial cell death has been hypothesized as an initiating mechanism underlying bleomycin-induced lung injury and fibrosis. In the present study we evaluated the contribution of mitochondrial and receptor-meditated death pathways in bleomycin-induced death of mouse alveolar epithelial cells (MLE-12 cells) and primary rat alveolar type II cells. Control MLE-12 cells and primary rat alveolar type II cells died after 48 h of exposure to bleomycin. Both MLE-12 cells and rat alveolar type II cells overexpressing Bcl-X(L) did not undergo cell death in response to bleomycin. Dominant negative Fas-associating protein with a death domain failed to prevent bleomycin-induced cell death in MLE-12 cells. Caspase-8 inhibitor CrmA did not prevent bleomycin-induced cell death in primary rat alveolar type II cells. Furthermore, fibroblast cells deficient in Bax and Bak, but not Bid, were resistant to bleomycin-induced cell death. To determine whether the stress kinase JNK was an upstream regulator of Bax activation, MLE-12 cells were exposed to bleomycin in the presence of an adenovirus encoding a dominant negative JNK. Bleomycin-induced Bax activation was prevented by the expression of a dominant negative JNK in MLE-12 cells. Dominant negative JNK prevented cell death in MLE-12 cells and in primary rat alveolar type II cells exposed to bleomycin. These data indicate that bleomycin induces cell death through a JNK-dependent mitochondrial death pathway in alveolar epithelial cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Animals
  • Antibiotics, Antineoplastic / pharmacology*
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • BH3 Interacting Domain Death Agonist Protein
  • Bleomycin / pharmacology*
  • Carrier Proteins / genetics
  • Cells, Cultured
  • Fas-Associated Death Domain Protein
  • Gene Expression
  • JNK Mitogen-Activated Protein Kinases / genetics
  • JNK Mitogen-Activated Protein Kinases / metabolism*
  • Membrane Proteins / genetics
  • Mice
  • Mice, Mutant Strains
  • Mitochondria / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Pulmonary Alveoli / cytology*
  • Pulmonary Alveoli / drug effects
  • Pulmonary Alveoli / enzymology
  • Rats
  • Respiratory Mucosa / cytology*
  • Respiratory Mucosa / drug effects
  • Respiratory Mucosa / enzymology
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-X Protein

Substances

  • Adaptor Proteins, Signal Transducing
  • Antibiotics, Antineoplastic
  • BH3 Interacting Domain Death Agonist Protein
  • Bak1 protein, mouse
  • Bak1 protein, rat
  • Bax protein, mouse
  • Bax protein, rat
  • Bcl2l1 protein, mouse
  • Bcl2l1 protein, rat
  • Bid protein, mouse
  • Bid protein, rat
  • Carrier Proteins
  • Fadd protein, mouse
  • Fadd protein, rat
  • Fas-Associated Death Domain Protein
  • Membrane Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • Bleomycin
  • JNK Mitogen-Activated Protein Kinases