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Erythropoietin Induces Tyrosine Phosphorylation of Jak2, STAT5A, and
STAT5B in Primary Cultured Human Erythroid Precursors
Atsushi Oda,
Kenichi Sawada,
Brian J. Druker,
Katsutoshi Ozaki,
Hina Takano,
Kazuki Koizumi,
Yoshikazu Fukada,
Makoto Handa,
Takao Koike, and
Yasuo Ikeda
From the Division of Hematology, Department of Internal Medicine,
Keio University, Tokyo, Japan; the Blood Center, Keio University,
Tokyo, Japan; The Department of Internal Medicine II, Hokkaido
University School of Medicine Sapporo, Hokkaido 060, Japan; and the
Division of Hematology and Medical Oncology, Oregon Health Sciences
University, Portland, OR.
We examined signaling by erythropoietin in highly purified human
colony forming unit-erythroid cells, generated in vitro from CD34+ cells. We found that erythropoietin induces
tyrosine phosphorylation of Jak2, STAT5A, and STAT5B. Tyrosine
phosphorylation of Jak2 reaches a peak around 10 minutes after
stimulation and is maximum at 5 U/mL of erythropoietin. Tyrosine
phosphorylation of STAT5 is accompanied by the translocation of
activated STAT5 to the nucleus as shown by electrophoretic mobility
shift assay (EMSA) using 32Pi-labeled STAT5 binding site in
the  -casein promoter. Tyrosine phosphorylation STAT1 or STAT3 was
not detected in human erythroid precursors after stimulation with
erythropoietin. Crkl, an SH2/SH3 adapter protein, becomes
coimmunoprecipitated specifically with STAT5 from
erythropoietin-stimulated erythroid cells; although it was shown to
become associated with c-Cbl in the studies using cell lines. Thus,
human erythroid precursors can be expanded in vitro in sufficient
numbers and purity to allow its usage in signal transduction studies.
This report sets a basis for further studies on signaling in primary
cultured human erythroid precursors, which in turn contribute to our
better understanding in the differentiation processes of erythrocytes
and their precursors.
Blood, Vol. 92 No. 2 (July 15), 1998:
pp. 443-451
© 1998 by the American Society of Hematology.
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