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Molecular basis of a high affinity murine interleukin-5 receptor

René Devos, Geert Plaetinck, José Van der Heyden, Sigrid Cornelis, Joël Vandekerckhove UGent, Walther Fiers UGent and Jan Tavernier UGent (1991) EMBO JOURNAL. 10(8). p.2133-2137
abstract
The mouse interleukin-5 receptor (mIL-5R) consists of two components one of which, the mIL-5R alpha-chain, binds mIL-5 with low affinity. Recently we demonstrated that monoclonal antibodies (Mabs) recognizing the second mIL-5R beta-chain, immunoprecipitate a pl30 - 140 protein doublet which corresponds to the mIL-3R and the mlL-3R-like protein, the latter chain for which so far no ligand has been identified. In this study we show that a high affinity mIL-5R can be reconstituted on COS1 cells by co-expression of the mIL-5R alpha-chain with the mIL-3R-like protein (beta-chain). Cross-linking of I-125-labeled mIL-5 to the COS1 cells co-transfected with both cDNAs revealed the same pattern as in B13 cells, i.e. two proteins of 60 and 130 kd which correspond to the low affinity mIL-5R alpha-chain and the mIL-3R-like protein, respectively. The dissociation rate of mIL-5 from this reconstituted high affinity site was lower than that of the low affinity site, whereas the association rate was unchanged. Nonetheless, the apparent dissociation constant (K(d)) for this reconstituted receptor was still 10-fold higher than the K(d) observed for B13 cells. Although the mIL-3R is > 90% homologous to the mIL-3R-like protein, no increase in affinity for mIL-5 was detected on COS1 cells co-transfected with the cDNAs for the mIL-5R alpha-chain and the mIL-3R protein.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
EOSINOPHILIA, CLONING, PROTEIN, EXPRESSION, GENE FAMILY, GM-CSF, CELL-LINE, MICE, TYROSINE PHOSPHORYLATION, COS1 CELL TRANSFECTION, HIGH AFFINITY RECEPTOR, MURINE IL-5 RECEPTOR, MURINE IL-3 RECEPTOR, COLONY-STIMULATING FACTOR, MURINE IL-3 RECEPTOR-LIKE
journal title
EMBO JOURNAL
Embo J.
volume
10
issue
8
pages
2133 - 2137
Web of Science type
Article
ISSN
0261-4189
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1925298
handle
http://hdl.handle.net/1854/LU-1925298
date created
2011-10-13 11:16:04
date last changed
2013-01-30 09:44:21
@article{1925298,
  abstract     = {The mouse interleukin-5 receptor (mIL-5R) consists of two components one of which, the mIL-5R alpha-chain, binds mIL-5 with low affinity. Recently we demonstrated that monoclonal antibodies (Mabs) recognizing the second mIL-5R beta-chain, immunoprecipitate a pl30 - 140 protein doublet which corresponds to the mIL-3R and the mlL-3R-like protein, the latter chain for which so far no ligand has been identified. In this study we show that a high affinity mIL-5R can be reconstituted on COS1 cells by co-expression of the mIL-5R alpha-chain with the mIL-3R-like protein (beta-chain). Cross-linking of I-125-labeled mIL-5 to the COS1 cells co-transfected with both cDNAs revealed the same pattern as in B13 cells, i.e. two proteins of 60 and 130 kd which correspond to the low affinity mIL-5R alpha-chain and the mIL-3R-like protein, respectively. The dissociation rate of mIL-5 from this reconstituted high affinity site was lower than that of the low affinity site, whereas the association rate was unchanged. Nonetheless, the apparent dissociation constant (K(d)) for this reconstituted receptor was still 10-fold higher than the K(d) observed for B13 cells. Although the mIL-3R is {\textrangle} 90\% homologous to the mIL-3R-like protein, no increase in affinity for mIL-5 was detected on COS1 cells co-transfected with the cDNAs for the mIL-5R alpha-chain and the mIL-3R protein.},
  author       = {Devos, Ren{\'e} and Plaetinck, Geert and Van der Heyden, Jos{\'e} and Cornelis, Sigrid and Vandekerckhove, Jo{\"e}l and Fiers, Walther and Tavernier, Jan},
  issn         = {0261-4189},
  journal      = {EMBO JOURNAL},
  keyword      = {EOSINOPHILIA,CLONING,PROTEIN,EXPRESSION,GENE FAMILY,GM-CSF,CELL-LINE,MICE,TYROSINE PHOSPHORYLATION,COS1 CELL TRANSFECTION,HIGH AFFINITY RECEPTOR,MURINE IL-5 RECEPTOR,MURINE IL-3 RECEPTOR,COLONY-STIMULATING FACTOR,MURINE IL-3 RECEPTOR-LIKE},
  language     = {eng},
  number       = {8},
  pages        = {2133--2137},
  title        = {Molecular basis of a high affinity murine interleukin-5 receptor},
  volume       = {10},
  year         = {1991},
}

Chicago
Devos, René, Geert Plaetinck, José Van der Heyden, Sigrid Cornelis, Joël Vandekerckhove, Walter Fiers, and Jan Tavernier. 1991. “Molecular Basis of a High Affinity Murine Interleukin-5 Receptor.” Embo Journal 10 (8): 2133–2137.
APA
Devos, René, Plaetinck, G., Van der Heyden, J., Cornelis, S., Vandekerckhove, J., Fiers, W., & Tavernier, J. (1991). Molecular basis of a high affinity murine interleukin-5 receptor. EMBO JOURNAL, 10(8), 2133–2137.
Vancouver
1.
Devos R, Plaetinck G, Van der Heyden J, Cornelis S, Vandekerckhove J, Fiers W, et al. Molecular basis of a high affinity murine interleukin-5 receptor. EMBO JOURNAL. 1991;10(8):2133–7.
MLA
Devos, René, Geert Plaetinck, José Van der Heyden, et al. “Molecular Basis of a High Affinity Murine Interleukin-5 Receptor.” EMBO JOURNAL 10.8 (1991): 2133–2137. Print.