The response to Histone deacetylase inhibitor in Imatinib resistant, BCR-ABL independent, K562 variant with high levels of phosphorylated P38

Background Imatinib mesylate, a TK inhibitor, is the main treatment for CML but patients may develop drug resistance. Mutations within the Abl kinase domain, increased expression of BCR-ABL or other regulatory mechanisms were suggested to be involved. However, recently the importance of Bcr-Abl independent mechanisms in Imatinib resistance was suggested. Exploring the role of proteins involved in Bcr-Abl independent resistance is of great importance in designing new modalities to overcome resistance or potentiate TKI efficacy.