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Thrombopoietin induces tyrosine phosphorylation of Stat3 and Stat5 in human
blood platelets
Y Miyakawa, A Oda, BJ Druker, H Miyazaki, M Handa, H Ohashi and Y Ikeda
Department of Internal Medicine, Keio University, Tokyo, Japan.
Thrombopoietin is known to be essential for megakaryocytopoiesis and
thrombopoiesis. Recently, we and others have shown that thrombopoietin
induces rapid tyrosine phosphorylation of Jak2 and other proteins in human
platelets and BaF3 cells, genetically engineered to express c- Mpl, a
receptor for thrombopoietin. The Jak family of tyrosine kinases are known
to mediate some of the effects of cytokines or hematopoietic growth factors
by recruitment and tyrosine phosphorylation of a variety of Stat (signal
transducers and activators of transcription) proteins. Hence, we have
investigated whether Stat proteins are present in platelets and, if so,
whether they become tyrosine phosphorylated in response to thrombopoietin.
We immunologically identified Stat1, Stat2, Stat3, and Stat5 in human
platelet lysates. Thrombopoietin induced tyrosine phosphorylation of Stat3
and Stat5 in these cells. Thrombopoietin also induced tyrosine
phosphorylation of Stat3 and Stat5 in FDCP-2 cells genetically engineered
to constitutively express human c-Mpl. Thus, our data indicate that Stat3
and Stat5 may be involved in signal transduction after ligand binding to
c-Mpl and that this event may have a role in
megakaryopoiesis/thrombopoiesis or possibly a mature platelet function such
as aggregation.
Volume 87,
Issue 2,
pp. 439-446,
01/15/1996
Copyright © 1996 by The American Society of Hematology
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