Biomolecules & Therapeutics

The Korean Society of Applied Pharmacology (한국응용약물학회)
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Influence of Environmental Conditions on c-Jun N-terminal Kinase Mediated Apoptosis of HL60 Cells by Anti-Cancer Drugs

  • Hur, Eun-Hye (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Kang, Mun-Jung (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Kim, Sung-Doo (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Lim, Sung-Nam (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Kim, Dae-Young (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Lee, Jung-Hee (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Lee, Kyoo-Hyung (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine) ;
  • Lee, Je-Hwan (Department of Hematology, Asan Medical Center, University of Ulsan College of Medicine)
  • Published : 2010.01.31
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Abstract

Activation of JNK has long been associated with the apoptotic response induced by various anti-cancer drugs including doxorubicin, vinblastine, and etoposide. In this study, we examined and compared patterns of apoptosis and JNK activation according to three different anti-cancer drugs (daunorubicin, vinblastine, and etoposide) and two different sources of HL60 cells (Jackson Laboratory and ATCC). HL60 cells from Jackson Laboratory (HL60/RPMI) were maintained in RPMI 1640 containing 5% fetal bovine serum and those from ATCC (HL60/IMDM) in IMDM containing 20% fetal bovine serum as to each manufacture's guideline. In general, HL60/RPMI cells were more sensitive to anti-cancer drugs compared to HL60/IMDM cells, demonstrated by the XTT and flow cytometric analyses. Apoptotic pathways after treatment with anti-cancer drugs seemed to be different between HL60/RPMI (daunorubicin and etoposide, caspase 3 dependent, but caspase 8 or 9 independent; vinblastine, caspase 3 independent) and HL60/IMDM (caspase 3 and caspase 9 dependent). The expression of apoptotic protein, BID, was consistent with caspase 3 activation. Immunoblotting of phospho-JNK and JNK kinase assay showed JNK activation by all three anti-cancer drugs in HL60/RPMI, while JNK activation was observed only in vinblastine-treated cells in HL60/IMDM. Our study results suggest that in vitro environmental conditions have a significant influence on JNK mediated apoptosis of HL60 cells by anti-cancer drugs and in vitro culture conditions are important factors in JNK or possibly other MAPK related studies.

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References

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