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1455806 
Journal Article 
The proteomic study of sodium butyrate antiproliferative/cytodifferentiation effects on K562 cells 
Grebenova, D; Kuzelova, K; Pluskalova, M; Peslova, G; Halada, P; Hrkal, Z 
2006 
Yes 
Blood Cells Molecules and Diseases
ISSN: 1079-9796 
37 
210-217 
English 
Employing methods of cell biology and proteome analysis tools, we examined effects of an inhibitor of histone deacetylases, sodium butyrate (SB), on the proliferation/differentiation characteristics of chronic myelogenous leukemia (CML)-derived cells K562. SB suppressed proliferation of K562 cells by inducing cell cycle arrest in G1 phase, which was followed by their transition to G0 phase (decrease of Ki-67 antigen-positive cells) and erythroid differentiation (increased glycophorin A expression and synthesis of hemoglobins). Neither terminal apoptosis (low counts of TUNEL-positive cells) nor necrosis (moderate counts of propidium iodide-positive cells) occurred. Importantly, SB attenuated protein expression of CML-related chimeric kinase BCR-ABL that is responsible for the deregulated proliferation of CML cells. The proteomic analysis (2-D electrophoresis combined with MALDI-TOF mass spectrometry and/or Western blotting) revealed several proteins that were differentially expressed or their mobility was altered due to butyrate treatment, namely, HSP90, HSP70, p23, cyclophilin A (CYPA), prefoldin2 (PFD2) and alpha-, gamma-, epsilon-human globin chains. Perturbation of HSP90 multichaperone complex of which BCR-ABL is the client protein is presumably a cause of BCR-ABL suppression. Changes in other proteins with chaperonic functions, CYPA and PFD2, may reflect SB antiproliferative and cytodifferentiation effects. 
K562; cell cycle; hemoglobin synthesis; BCR-ABL; proteome analysis; HSP90; p23; CYP-A; prefoldin2 
IRIS
• n-Butanol
     Database searches
          WOS
     Source – January 2013 (private)
          WOS - 1/2013
          Merged reference set - 1/2013
     Excluded (not pertinent)
          Miscellaneous