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Tyrosine phosphorylation and activation of JAK family tyrosine kinases by
interleukin-9 in MO7E cells
T Yin, L Yang and YC Yang
Walther Oncology Center, Indiana University Medical Center, Indianapolis
46202, USA.
Interleukin-9 (IL-9) is a T-cell-derived multifunctional cytokine that can
stimulate the proliferation of a human megakaryocytic leukemia cell line,
MO7E. Previous studies suggested that protein tyrosine phosphorylation may
be involved in IL-9 signaling pathways. However, tyrosine kinases activated
by IL-9 have not been identified. In this report we show that IL-9 induces
tyrosine phosphorylation and activation of the JAK family tyrosine kinases
including JAK1, JAK3, and Tyk2. The kinetic studies indicate that tyrosine
phosphorylation and activation of JAK kinases induced by IL-9 occurred
within 1 minute, peaked by 5 to 10 minutes, and persisted at least for 45
minutes. Furthermore, we show that signal transducers and activators of
transcription (Stat) 91 or related protein and an 88-kD Stat 91- associated
protein are rapidly tyrosine phosphorylated following IL-9 treatment. Gel
shift assays confirm that nuclear extracts from MO7E cells stimulated with
IL-9 specifically interact with a DNA element termed gamma activated site.
These results suggest that actions of IL-9 may, in part, be mediated
through JAK kinase-Stat signaling cascades.
Volume 85,
Issue 11,
pp. 3101-3106,
06/01/1995
Copyright © 1995 by The American Society of Hematology
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