Evidence map›Paper›PMID 8496674›Full record

ArticleThe Journal of experimental medicine1993

Reconstitution of the functional receptors for murine and human interleukin 5.

S Takaki, Y Murata, T Kitamura, A Miyajima, A Tominaga, K Takatsu

Abstract read
In one paragraph

Article in The Journal of experimental medicine, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
  2. Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012
    Article
  3. Interleukin-5 and IL-5 receptor in health and diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011
    Review
  4. Article
  5. Article
  6. Crystallization and preliminary X-ray diffraction analysis of the ternary human GM-CSF receptor complex.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  14. Article
  15. Article
  16. Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  17. Article
  18. Article
  19. Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

S TakakiDepartment of Immunology, University of Tokyo, Japan.
Y Murata
T Kitamura
A Miyajima
A Tominaga
K Takatsu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The murine interleukin 5 receptor (mIL-5R) is composed of two distinct subunits, alpha and beta. The alpha subunit (mIL-5R alpha) specifically binds IL-5 with low affinity. The beta subunit (mIL-5R beta) does not bind IL-5 by itself, but forms the high-affinity receptor with mIL-5R alpha. mIL-5R beta has been revealed to be the mIL-3R-like protein, AIC2B which is shared with receptors for IL-3 and granulocyte/macrophage colony-stimulating factor. We demonstrated here the reconstitution of the functional receptors for murine and human IL-5 on the mouse IL-2-dependent cell line, CTLL-2. CTLL-2 was transfected with the cDNAs for mIL-5R alpha and/or AIC2B. Only CTLL-2 transfectant expressing both mIL-5R alpha and AIC2B expressed the high-affinity receptor and proliferated in response to murine IL-5. Then CTLL-2 was transfected with the cDNAs for hIL-5R alpha and/or KH97 (beta c), the human homologue of AIC2B. Though beta c did not contribute much to binding affinity of hIL-5R, only CTLL-2 transfectant expressing both hIL-5R alpha and beta c proliferated in response to human IL-5. These results showed that the beta subunit is indispensable in IL-5 signal transduction. We further investigated the function of IL-5-specific alpha subunit in transmitting IL-5 signals. Mutant mIL-5R alpha, which lacks its whole cytoplasmic domain, was transfected into mouse IL-3-dependent cell line, FDC-P1 expressing AIC2B intrinsically. The resulting transfectant did not respond to IL-5, though the transfectant expressed the high-affinity IL-5R, indicating that the cytoplasmic portion of the alpha subunit also has some important role in IL-5-mediated signal transduction.

Indexed as

Receptors, InterleukinAnimalsBase SequenceCell LineHumansInterleukin-2Interleukin-5MiceMolecular Sequence DataReceptors, ImmunologicReceptors, Interleukin-5Signal TransductionTransfectionInterleukin-2Interleukin-5Receptors, ImmunologicReceptors, InterleukinReceptors, Interleukin-5

Identifiers

PMID8496674
PMCPMC2191058

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.