Thrombopoietin induces tyrosine phosphorylation of Stat3 and Stat5 in human blood platelets

Yoshitaka Miyakawa, Atsushi Oda, Brian J. Druker, Hiroshi Miyazaki, Makoto Handa, Hideya Ohashi, Yasuo Ikeda

Research output: Contribution to journalArticlepeer-review

163 Scopus citations

Abstract

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-MpI, 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 Slat 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-MpI. Thus, our data indicate that Stat3 and Stat5 may be involved in signal transduction after ligand binding to c-MpI and that this event may have a role in megakaryopoiesis/thrombopoiesis or possibly a mature platelet function such as aggregation.

Original languageEnglish (US)
Pages (from-to)439-446
Number of pages8
JournalBlood
Volume87
Issue number2
DOIs
StatePublished - Jan 15 1996

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

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