Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/8692
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Barry, S. | - |
dc.contributor.author | Korpelainen, E. | - |
dc.contributor.author | Sun, Q. | - |
dc.contributor.author | Stomski, F. | - |
dc.contributor.author | Moretti, P. | - |
dc.contributor.author | Wakao, H. | - |
dc.contributor.author | D'Andrea, R. | - |
dc.contributor.author | Vadas, M. | - |
dc.contributor.author | Lopez, A. | - |
dc.contributor.author | Goodall, G. | - |
dc.date.issued | 1997 | - |
dc.identifier.citation | Blood, 1997; 89(3):842-852 | - |
dc.identifier.issn | 0006-4971 | - |
dc.identifier.issn | 1528-0020 | - |
dc.identifier.uri | http://hdl.handle.net/2440/8692 | - |
dc.description | Copyright © 1997 by The American Society of Hematology | - |
dc.description.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. | - |
dc.description.statementofresponsibility | 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 | - |
dc.language.iso | en | - |
dc.publisher | W B SAUNDERS CO | - |
dc.source.uri | http://bloodjournal.hematologylibrary.org/cgi/reprint/89/3/842 | - |
dc.subject | COS Cells | - |
dc.subject | Cytoplasm | - |
dc.subject | Intracellular Fluid | - |
dc.subject | Animals | - |
dc.subject | Receptors, Interleukin-3 | - |
dc.subject | Antibodies, Blocking | - |
dc.subject | Antibodies, Monoclonal | - |
dc.subject | Signal Transduction | - |
dc.subject | Mutagenesis | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Protein Structure, Tertiary | - |
dc.subject | Protein Binding | - |
dc.title | Roles of the N and C terminal domains of the interleukin-3 receptor alpha chain in receptor function. | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1182/blood.v89.3.842 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Barry, S. [0000-0002-0597-7609] | - |
dc.identifier.orcid | Lopez, A. [0000-0001-7430-0135] | - |
dc.identifier.orcid | Goodall, G. [0000-0003-1294-0692] | - |
Appears in Collections: | Aurora harvest Medicine publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.