The Inhibition of Hsp27 Chaperone Affects the Level of p53 Protein in Tumor Cells


  •  E. Kaigorodova    
  •  L. Litvinova    
  •  E. Konovalova    
  •  M. Klimova    
  •  L. Tashireva    
  •  O. Nosareva    
  •  V. Novitskiy    

Abstract

The characteristics of p53 protein content in Jurkat and THP-1 tumor cell line, and mononuclear leukocytes were evaluated from in vitro studies with selective inhibition of the chaperone Hsp27. For the inhibition of Hsp27 KRIBB3 ((5-(5-ethyl-2-hydroxy-4-methoxyphenyl)-4-(4-methoxyphenyl)-isoxasole) was used. The p53 protein concentration was determined by Western blot analysis. The apoptoticly transformed cells with selective inhibitor Hsp27 were assessed by in vitro fluorescence microscopy using FITC-labeled annexin V and propidium iodide. The present study showed that the in vitro inhibition of the chaperone Hsp27 leads to an increase in p53 concentration in tumor cells and a growth of the amount of apoptotic cells in modified Jurkat and THP-1 cultures but revealed no such effects in the mononuclear leukocytes culture. Thus, Hsp27 appeared to play an important regulatory role in the activation of p53 protein of tumor cells.



This work is licensed under a Creative Commons Attribution 4.0 License.
  • Issn(Print): 1916-9671
  • Issn(Onlne): 1916-968X
  • Started: 2009
  • Frequency: quarterly

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