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Recombinant thrombopoietin induces rapid protein tyrosine phosphorylation
of Janus kinase 2 and Shc in human blood platelets
Y Miyakawa, A Oda, BJ Druker, T Kato, H Miyazaki, M Handa and Y Ikeda
Department of Internal Medicine, Keio University, Tokyo, Japan.
A cDNA for the thrombopoietin has been cloned by several groups. The
recombinant thrombopoietin has been reported to stimulate the
megakaryocytopoiesis and thrombopoiesis. Little is known regarding the
molecular basis of its effects. To elucidate the molecular mechanism
involved in signal transduction, we have investigated the effects of
thrombopoietin on platelet tyrosine phosphorylation. We report here that
thrombopoietin induced time- and dose-dependent tyrosine phosphorylation of
several proteins including Janus kinase 2 (Jak2) and a 52-kD protein, Shc,
in human blood platelets. Both Jak2 and Shc were tyrosine phosphorylated
within 15 seconds after stimulation. The tyrosine phosphorylation of Jak2
was accompanied by increased kinase activity, whereas Shc tyrosine
phosphorylation induced its association with a 25-kD protein, Grb2. Thus,
our data suggest that Jak2, Shc, and Grb2 may be involved in signal
transduction after ligand binding to c- mpl in human platelets.
Volume 86,
Issue 1,
pp. 23-27,
07/01/1995
Copyright © 1995 by The American Society of Hematology
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