Signaling pathways and functions in primary human myelogenous leukemic cells stimulated by cytokines.
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概要
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We investigated tyrosine phosphorylation of proteins in primary human acute myelogenous leukemia (AML) cells stimulated by cytokines (G-CSF, GM-CSF, TNF, M-CSF, IL-3 and SCF) .These cytokines induced protein tyrosine phosphorylation in 14-17 cases out of total 18 cases tested, except that M-CSF induced this response only in 9 cases. In the present study, we observed cytokine-specific pattern of tyrosine phosphorylation of proteins in all cases. GM-CSF and IL-3 induced tyrosine phosphorylation of p92, p80, p70 and p42. In addition to these proteins, p95 was specifically tyrosine-phosphorylated by G-CSF in most of G-CSF-responsive cases. SCF induced tyrosine phosphorylation of p140-200, p110, p95, p60, p55 and p42, and M-CSF induced tyrosine phosphorylation of p140-200, p110 and p42. On the other hand, TNF exclusively induced tyrosine phosphorylation p42. p92 was identified as c-fes product in some cases, but was found to be STAT 5 in the other cases. p95 was identified as vav product in all cases tested. p42 and p140-200 (in M-CSF stimulation) was identified as microtubule-associated protein kinase and c-fms product, respectively.<BR>Respiratory burst activity of abnormal neutrophils in patients with myeloproliferative disorders such as chronic myelogenous leukemia was also investigated. In these patients, superoxide-producing capacity of neutrophils was markedly increased as compared with normal neutrophils. This phenomenon was observed only when neutrophils were stimulated with receptor-mediated agonists to release superoxide, and superoxide release induced by phorbol ester was normal in patients. In addition, <I>in vitro</I> responsiveness of patient neutrophils to cytokines was decreased. These findings suggest <I>in vivo</I> priming and activation of neutrophils by cytokines or via related mechanism in patients with myeloproliferative disorders.
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