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A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF

Jan Tavernier UGent, René Devos, Sigrid Cornelis, Tania Tuypens, José Van der Heyden, Walter Fiers UGent and Geert Plaetinck (1991) CELL. 66(6). p.1175-1184
abstract
cDNA clones encoding two receptor proteins involved in the binding of human interleukin 5 (hIL5) have been isolated. A first class codes for an IL5-specific chain (hIL5R-alpha). The major transcript of this receptor gene, as analyzed in both HL-60 eosinophilic cells and eosinophilic myelocytes grown from cord blood, encodes a secreted form of this receptor. This soluble hIL5R-alpha has antagonistic properties. A second component of the hIL5R is found to be identical to the beta-chain of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) high affinity receptor. The finding that IL5 and GM-CSF share a receptor subunit provides a molecular basis for the observation that these cytokines can partially interfere with each other's binding and have highly overlapping biological activities on eosinophils.
Please use this url to cite or link to this publication:
author
organization
alternative title
A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF
year
type
journalArticle (original)
publication status
published
subject
keyword
EOSINOPHIL DIFFERENTIATION FACTOR, COLONY-STIMULATING FACTOR, MOLECULAR-CLONING, HISTAMINE-RELEASE, SOLUBLE FORM, GENE FAMILY, HUMAN-URINE, EXPRESSION, BINDING, CELLS
journal title
CELL
Cell
volume
66
issue
6
pages
1175 - 1184
Web of Science type
Article
ISSN
0092-8674
DOI
10.1016/0092-8674(91)90040-6
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
221628
handle
http://hdl.handle.net/1854/LU-221628
date created
2004-05-24 13:24:00
date last changed
2011-11-10 09:20:12
@article{221628,
  abstract     = {cDNA clones encoding two receptor proteins involved in the binding of human interleukin 5 (hIL5) have been isolated. A first class codes for an IL5-specific chain (hIL5R-alpha). The major transcript of this receptor gene, as analyzed in both HL-60 eosinophilic cells and eosinophilic myelocytes grown from cord blood, encodes a secreted form of this receptor. This soluble hIL5R-alpha has antagonistic properties. A second component of the hIL5R is found to be identical to the beta-chain of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) high affinity receptor. The finding that IL5 and GM-CSF share a receptor subunit provides a molecular basis for the observation that these cytokines can partially interfere with each other's binding and have highly overlapping biological activities on eosinophils.},
  author       = {Tavernier, Jan and Devos, Ren{\'e} and Cornelis, Sigrid and Tuypens, Tania and Van der Heyden, Jos{\'e} and Fiers, Walter and Plaetinck, Geert},
  issn         = {0092-8674},
  journal      = {CELL},
  keyword      = {EOSINOPHIL DIFFERENTIATION FACTOR,COLONY-STIMULATING FACTOR,MOLECULAR-CLONING,HISTAMINE-RELEASE,SOLUBLE FORM,GENE FAMILY,HUMAN-URINE,EXPRESSION,BINDING,CELLS},
  language     = {eng},
  number       = {6},
  pages        = {1175--1184},
  title        = {A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific \ensuremath{\alpha} chain and a \ensuremath{\beta} chain shared with the receptor for GM-CSF},
  url          = {http://dx.doi.org/10.1016/0092-8674(91)90040-6},
  volume       = {66},
  year         = {1991},
}

Chicago
Tavernier, Jan, René Devos, Sigrid Cornelis, Tania Tuypens, José Van der Heyden, Walter Fiers, and Geert Plaetinck. 1991. “A Human High Affinity Interleukin-5 Receptor (IL5R) Is Composed of an IL5-specific α Chain and a β Chain Shared with the Receptor for GM-CSF.” Cell 66 (6): 1175–1184.
APA
Tavernier, Jan, Devos, R., Cornelis, S., Tuypens, T., Van der Heyden, J., Fiers, W., & Plaetinck, G. (1991). A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF. CELL, 66(6), 1175–1184.
Vancouver
1.
Tavernier J, Devos R, Cornelis S, Tuypens T, Van der Heyden J, Fiers W, et al. A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF. CELL. 1991;66(6):1175–84.
MLA
Tavernier, Jan, René Devos, Sigrid Cornelis, et al. “A Human High Affinity Interleukin-5 Receptor (IL5R) Is Composed of an IL5-specific α Chain and a β Chain Shared with the Receptor for GM-CSF.” CELL 66.6 (1991): 1175–1184. Print.