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https://hdl.handle.net/2440/8692
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Type: | Journal article |
Title: | Roles of the N and C terminal domains of the interleukin-3 receptor alpha chain in receptor function. |
Author: | Barry, S. Korpelainen, E. Sun, Q. Stomski, F. Moretti, P. Wakao, H. D'Andrea, R. Vadas, M. Lopez, A. Goodall, G. |
Citation: | Blood, 1997; 89(3):842-852 |
Publisher: | W B SAUNDERS CO |
Issue Date: | 1997 |
ISSN: | 0006-4971 1528-0020 |
Statement of Responsibility: | S.C. Barry, E. Korpelainen, Q. Sun, F.C. Stomski, P.A.B. Moretti, H. Wakao, R.J. D’Andrea, M.A. Vadas, A.F. Lopez, and G.J. Goodall |
Abstract: | The interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and IL-5 receptor alpha chains are each composed of three extracellular domains, a transmembrane domain and a short intracellular region. Domains 2 and 3 constitute the cytokine receptor module (CRM), typical of the cytokine receptor superfamily; however, the function of the N-terminal domain is not known. We have investigated the functions of the N-terminal and C-terminal domains of the IL-3 receptor (IL-3R) alpha chain. We find that cells transfected with the receptor beta chain (h beta c) and a truncated IL-3R alpha that is devoid of the intracellular region fail to proliferate or to activate STAT5 in response to human IL-3, despite binding the IL-3 with affinity indistinguishable from that of full-length receptor. In addition, IL-3-induced phosphorylation of h beta c was not detected. Thus, the IL-3R alpha intracellular region does not contribute detectably to stabilization of the receptor/ligand complex, but is essential for signal propagation. In contrast, a truncated IL-3R alpha with the N-terminal domain deleted interacts functionally with the beta chain; mouse cells transfected with these receptor chains proliferate in response to human IL-3 and STAT5 transcription factor is activated. High- and low-affinity binding sites are retained, although the affinity for IL-3 is decreased 15-fold, indicating a significant role for the N-terminal domain in IL-3 binding. |
Keywords: | COS Cells Cytoplasm Intracellular Fluid Animals Receptors, Interleukin-3 Antibodies, Blocking Antibodies, Monoclonal Signal Transduction Mutagenesis Amino Acid Sequence Protein Structure, Tertiary Protein Binding |
Description: | Copyright © 1997 by The American Society of Hematology |
DOI: | 10.1182/blood.v89.3.842 |
Published version: | http://bloodjournal.hematologylibrary.org/cgi/reprint/89/3/842 |
Appears in Collections: | Aurora harvest Medicine publications |
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