A possible involvement of Stat5 in erythropoietin-induced hemoglobin synthesis

Biochemical and Biophysical Research Communications
H WakaoA Miyajima

Abstract

Erythropoietin (EPO) and its cell surface receptor (EPOR) play central roles in the proliferation and differentiation of mammalian erythroid progenitor cells. Recently both the tyrosine residues in the EPOR responsible for the activation of Stat5 and the role of Stat5 for EPO-dependent cell proliferation have been shown. Here, we describe the roles of Stat5 and of these tyrosine residues in the EPOR in the erythroid differentiation of murine hematopoietic cell line SKT6 which produces hemoglobin in response to EPO. Chimeric receptors carrying the extracellular domain of the EGF receptor and the intracellular domain of the EPOR were introduced into SKT6 cells. Like EPO, EGF equally activated Stat5 and induced hemoglobin. Activation of Stat5 and hemoglobin expression by EGF were markedly impaired in cells expressing the tyrosine mutated chimeric receptors. In addition, ectopic expression of the prolactin receptor, another cytokine receptor that activates Stat5, led to hemoglobin synthesis. Finally, hemoglobin synthesis was severely inhibited by overexpressing a dominant negative form of Stat5. These results collectively suggest that Stat5 plays a role in EPO-mediated hemoglobin synthesis in SKT6 cells.

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Citations

Oct 31, 2000·Bioscience, Biotechnology, and Biochemistry·R SasakiM Nagao
May 22, 2007·Biochemical and Biophysical Research Communications·Akemi Hoshino, Hodaka Fujii
Dec 2, 1999·Experimental Cell Research·D M WojchowskiT J Pircher
Oct 30, 2008·Journal of Immunotoxicology·Hodaka Fujii
Aug 4, 2005·Chronobiology International·Rachel Ben-ShlomoCharalambos P Kyriacou
Sep 25, 1999·Growth Factors·P A Tilbrook, S P Klinken

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