Bombesin activates MAP kinase in non-small cell lung cancer cells

Peptides. 1999;20(1):121-6. doi: 10.1016/s0196-9781(98)00144-2.


The effects of bombesin (BB) on mitogen activated protein (MAP) kinase were investigated using non-small cell lung cancer (NSCLC) cells. By Western blot, both 42 and 44 kDalton forms of MAP kinase were present in NCI-H1299 and NCI-H838 cells. Addition of BB to NCI-H1299 cells resulted in phosphorylation of the MAP kinase substrate myelin basic protein (MBP). Phosphorylation of MBP was maximal 6 min after the addition of 10 nM BB to NCI-H1299 cells. Addition of gastrin releasing peptide (GRP) or GRP14-27 but not GRP1-16 to NCI-H 1299 cells caused MBP phosphorylation. The effects of BB were inhibited by BW2258U89, a BB receptor antagonist, and PD98059, a MAP kinase kinase inhibitor. Also, PD98059 inhibited the clonal growth of NCI-H1299 cells. These data suggest that MAP kinase may be an important regulatory enzyme in NSCLC.

MeSH terms

  • Amino Acid Sequence
  • Bombesin / metabolism*
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Carcinoma, Non-Small-Cell Lung / enzymology*
  • Carcinoma, Non-Small-Cell Lung / pathology
  • Gastrin-Releasing Peptide / pharmacology
  • Humans
  • Lung Neoplasms / enzymology*
  • Lung Neoplasms / pathology
  • Molecular Sequence Data
  • Phosphorylation / drug effects
  • Tumor Cells, Cultured


  • Gastrin-Releasing Peptide
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Bombesin