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• W1041014198 abstract "BCR/ABL transforms hematopoietic cells in vitro and in vivo and exerts a wide variety of biological effects, including induction of factor independence, reduction of apoptosis, and altering adhesion of CML cells to marrow stroma. However, at a biochemical level, the mechanisms by which BCR/ABL transforms myeloid cells are poorly understood. p210BCR/ABL has elevated ABL tyrosine kinase activity, relocates to the cytoskeleton, and phosphorylates several cellular proteins, including c-BCR, pl20rasGAP, c-CBL, p52SHC, p93FES, p95VAV, pl25FAK, p68paxillin, and p72SH PTP2. In addition, BCR/ABL has been shown to bind directly to GRB2 at Y177 of BCR, therefore potentially activating p21ras. However, it has been difficult to determine the significance of any of these potential BCR/ABL substrates, in part due to the complexity of studying a large protein with many potential signaling motifs, and in part due to the fact that there are so many BCR/ABL substrates in these cell lines. One approach to simplifying BCR/ABL biology has been to examine primary human CML cells, rather than cell lines made to overexpress BCR/ABL. Interestingly, in primary leukemic cells, there are only a few proteins which either intereact with BCR/ABL or are phosphorylated by BCR/ABL. This suggests that studies in primary CML cells, rather than tissue culture cell lines, may be more reliable in terms of identifying important signaling pathways. One of the major tyrosine phosphoproteins complexed with BCR/ABL in CML neutrophils has recently been identified as CRKL, an SH2/SH3 “adapter” protein. CRKL binds to BCR/ABL at least partly through its SH3 domain, and in cell lines may link BCR/ABL to some cytoskeletal proteins. The hypothesis hypothesis is set forth that BCR/ABL functions in part to disrupt signals going to, or coming from integrins in hematopoietic cells, and that this event is important in the pathogenesis of stable phase CML." @default.
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• W1041014198 date "1997-01-01" @default.
• W1041014198 modified "2023-09-24" @default.
• W1041014198 title "BCR/ABL and Signal Transduction Pathways" @default.
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• W1041014198 doi "https://doi.org/10.1007/978-3-642-60377-8_26" @default.
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