Evidence map›Paper›PMID 1732409›Full record

ArticleThe Journal of experimental medicine1992

Molecular cloning and expression of the human interleukin 5 receptor.

Y Murata, S Takaki, M Migita, Y Kikuchi, A Tominaga, K Takatsu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
7.4field-weighted citation impact, top 2% of its field
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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 199 citations in OpenAlex.

  1. Pooled it
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  7. Review
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  10. Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012
    Article
  11. Article
  12. Interleukin-5 and IL-5 receptor in health and diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011
    Review
  13. Article
  14. Cord blood molecular biomarkers of eosinophilopoiesis: kinetic analysis of GATA-1, MBP1 and IL-5R alpha mRNA expression.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2010
    Article
  15. 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
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  17. Review
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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 at 1 institution in 1 country.

Y MurataDepartment of Biology, Kumamoto University Medical School, Japan.
S Takaki
M Migita
Y Kikuchi
A Tominaga
K Takatsu
Kumamoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human interleukin 5 (IL-5) plays an important role in proliferation and differentiation of human eosinophils. We report the isolation of cDNA clones from cDNA libraries of human eosinophils by using murine IL-5 receptor alpha chain cDNA as a probe. Analysis of the predicted amino acid sequence indicated that the human IL-5 receptor has approximately 70% amino acid sequence homology with the murine IL-5 receptor and retains features common to the cytokine receptor superfamily. One cDNA clone encodes a glycoprotein of 420 amino acids (Mr 47,670) with an NH2-terminal hydrophobic region (20 amino acids), a glycosylated extracellular domain (324 amino acids), a transmembrane domain (21 amino acids), and a cytoplasmic domain (55 amino acids). Another cDNA encodes only the extracellular domain of this receptor molecule. Other cDNA clones encode molecules having diversified cytoplasmic domains. COS7 cells transfected with the cDNA expressed a approximately 60-kD protein and bound IL-5 with a single class of affinity (Kd = 250-590 pM). The Kd values were similar to that observed in normal human eosinophils. In contrast to the murine 60-kD alpha chain, which binds IL-5 with low affinity (Kd = approximately 10 nM), the human alpha chain homologue can bind IL-5 with much higher affinity by itself. RNA blot analysis of human cells demonstrated two transcripts (approximately 5.3 and 1.4 kb). Both of them were expressed in normal human eosinophils and in erythroleukemic cell line TF-1, which responds to IL-5. The human IL-5 receptor characterized in this paper is essential for signal transduction, because expression of this molecule in murine IL-3-dependent cell line FDC-P1 allowed these cells to proliferate in response to IL-5.

Indexed as

Receptors, InterleukinAmino Acid SequenceAnimalsBase SequenceCell LineCloning, MolecularDNADNA ProbesEosinophilsGene ExpressionHumansInterleukin-5MiceMolecular Sequence DataNucleic Acid HybridizationReceptors, ImmunologicDNADNA ProbesInterleukin-5Receptors, ImmunologicReceptors, InterleukinReceptors, Interleukin-5Recombinant ProteinsRNA, Messenger

Identifiers

PMID1732409
PMCPMC2119102
OpenAlexW2161335440

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.