v-Abl protein tyrosine kinase (PTK) mediated suppression of apoptosis is associated with the up-regulation of Bcl-XL

Q Chen, J Turner, A J Watson, C Dive

Research output: Contribution to journalArticlepeer-review


We demonstrated previously that the activation of v-Abl protein tyrosine kinase (PTK) in IC.DP murine pre-mast cells resulted in suppression of apoptosis after withdrawal of interleukin 3 (IL-3), that protein kinase C (PKC) translocated to the nucleus 6 h after v-Abl PTK activation and that inhibition of PKC restored apoptosis after IL-3 deprivation in the presence of v-Abl PTK activity. Here we demonstrate that v-Abl PTK activation is followed by an approximately twofold increase in mRNA level of Bcl-XL by 6 h and a corresponding increase in Bcl-XL protein level by 24 h. Bcl-xL RNA and protein decreased in IL-3 deprived cells in the absence of v-Abl PTK activity. Exposure of cells with v-Abl PTK active to the PKC inhbitor calphostin C (125 ng/ml) prevented the increase in Bcl-xL protein and resulted in apoptosis. No changes in Bax or Bcl-2 protein level were noted after IL-3 withdrawal and/or activation of v-Abl PTK. Bak was barely detectable and Bad protein level decreased in cells undergoing apoptosis. The data suggest that suppression of apoptosis by v-Abl PTK in the absence of IL-3 is associated with PKC signalling and the upregulation of Bcl-xL in IC.DP cells.
Original languageEnglish
Pages (from-to)2249-54
Number of pages2194
Issue number18
Publication statusPublished - 1997


  • Animals
  • Apoptosis/*physiology
  • Cell Line
  • Enzyme Activation
  • Flow Cytometry
  • Interleukin-3/deficiency
  • Mast Cells/enzymology/metabolism
  • Mice
  • Protein-Tyrosine Kinases/*metabolism
  • Proto-Oncogene Proteins c-abl/*metabolism
  • Proto-Oncogene Proteins c-bcl-2/*biosynthesis
  • RNA, Messenger/metabolism
  • Up-Regulation/physiology
  • bcl-X Protein


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