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Recombinant human interleukin-9 induces protein tyrosine phosphorylation
and synergizes with steel factor to stimulate proliferation of the human
factor-dependent cell line, M07e
K Miyazawa, PC Hendrie, YJ Kim, C Mantel, YC Yang, BS Kwon and HE Broxmeyer
Department of Medicine (Hematology/Oncology), Indiana University School of
Medicine, Indianapolis 46202-5121.
Human interleukin-9 (IL-9) was originally identified and cloned based on
its stimulatory effect on proliferation of human myeloid cell line, M07e.
IL-9 synergized with Steel factor, the ligand for the c-kit product, to
stimulate M07e cell proliferation. To investigate potential mechanisms for
this, IL-9 was assessed for effects on protein tyrosine kinase activities
in M07e cells by immunoblotting with anti- phosphotyrosine monoclonal
antibody; results were compared with those of Steel factor alone and in
combination with IL-9, and those of 12-0- tetradecanoyl phorbol-13-acetate
(TPA). Recombinant human IL-9 (10 ng/mL) rapidly and transiently induced or
enhanced at least four tyrosine phosphorylated protein bands with molecular
weights of 105, 97, 85, and 81 Kd. This tyrosine phosphorylation pattern
was different from that generated by recombinant murine Steel factor or TPA
stimulation and the combination of IL-9 and Steel factor did not change the
IL-9-induced pattern. IL-9-induced tyrosine phosphorylated bands were
completely blocked by treatment of IL-9 with anti-IL-9 antibody under
conditions that also neutralized the synergistic effect of IL-9 with Steel
factor on M07e cell proliferation. Genistein, a tyrosine kinase inhibitor,
blocked phosphorylation of IL-9 and Steel factor- induced bands. Unlike
Steel factor or TPA, IL-9 did not appear to stimulate phosphorylation of
42-Kd mitogen-activated protein (MAP) kinase or Raf-1, or enhance MAP
kinase activity. MAP kinase and Raf-1 are serine/threonine kinases that are
phosphorylated and activated by many growth factors and by agonists for
protein kinase C. While the combination of IL-9 plus SLF did not appear to
induce phosphorylation of new bands not already seen with either IL-9 or
SLF alone, or enhance the phosphorylation of those bands seen with either
cytokine alone, the results suggest that IL-9 activates specific and unique
signal transduction pathways.
Volume 80,
Issue 7,
pp. 1685-1692,
10/01/1992
Copyright © 1992 by The American Society of Hematology
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