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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

(1991) CELL. 66(6). p.1175-1184
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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.
Keywords
EOSINOPHIL DIFFERENTIATION FACTOR, COLONY-STIMULATING FACTOR, MOLECULAR-CLONING, HISTAMINE-RELEASE, SOLUBLE FORM, GENE FAMILY, HUMAN-URINE, EXPRESSION, BINDING, CELLS

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Citation

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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.
@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},
}

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