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A possible involvement of Stat5 in erythropoietin-induced hemoglobin synthesis.
Biochem Biophys Res Commun. 1997 May 08; 234(1):198-205.BB

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.

Authors+Show Affiliations

Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan. hwakao@hri.co.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9168989

Citation

Wakao, H, et al. "A Possible Involvement of Stat5 in Erythropoietin-induced Hemoglobin Synthesis." Biochemical and Biophysical Research Communications, vol. 234, no. 1, 1997, pp. 198-205.
Wakao H, Chida D, Damen JE, et al. A possible involvement of Stat5 in erythropoietin-induced hemoglobin synthesis. Biochem Biophys Res Commun. 1997;234(1):198-205.
Wakao, H., Chida, D., Damen, J. E., Krystal, G., & Miyajima, A. (1997). A possible involvement of Stat5 in erythropoietin-induced hemoglobin synthesis. Biochemical and Biophysical Research Communications, 234(1), 198-205.
Wakao H, et al. A Possible Involvement of Stat5 in Erythropoietin-induced Hemoglobin Synthesis. Biochem Biophys Res Commun. 1997 May 8;234(1):198-205. PubMed PMID: 9168989.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A possible involvement of Stat5 in erythropoietin-induced hemoglobin synthesis. AU - Wakao,H, AU - Chida,D, AU - Damen,J E, AU - Krystal,G, AU - Miyajima,A, PY - 1997/5/8/pubmed PY - 1997/5/8/medline PY - 1997/5/8/entrez SP - 198 EP - 205 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 234 IS - 1 N2 - 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. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/9168989/A_possible_involvement_of_Stat5_in_erythropoietin_induced_hemoglobin_synthesis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(97)96486-X DB - PRIME DP - Unbound Medicine ER -