Evidence map›Paper›PMID 1711211›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Localized cytosolic domains of the erythropoietin receptor regulate growth signaling and down-modulate responsiveness to granulocyte-macrophage colony-stimulating factor.

D E Quelle, D M Wojchowski

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
11.0field-weighted citation impact, top 1% 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

22 citing papers in PubMed, 94 citations in OpenAlex.

  1. Erythropoietin receptor response circuits.Current opinion in hematology · 2010
    Review
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  6. A proliferation switch for genetically modified cells.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
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  8. Article
  9. Activated Ki-Ras complements erythropoietin signaling in CTLL-2 cells, inducing tyrosine phosphorylation of a 160-kDa protein.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  10. Article
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  13. Mutational analysis of a critical signaling domain of the human interleukin 4 receptor.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  14. Article
  15. Article
  16. Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  17. Isolation of interleukin 2-induced immediate-early genes.Proceedings of the National Academy of Sciences of the United States of America · 1993
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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

2 authors at 1 institution in 1 country.

D E QuelleDepartment of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
D M Wojchowski
Pennsylvania State University · US

Funding

IN VITRO STUDIES OF ERYTHROPOIETIN ACTIONR01HL044491 · NHLBI · UNIVERSITY OF NEW HAMPSHIRE · PI WOJCHOWSKI, DON MICHAEL · 1991 to 2020
$4.8M
BIOCHEMISTRY OF THE ERYTHROPOIETIN RECEPTORR29DK040242 · NIDDK · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI WOJCHOWSKI, DON · 1988 to 1992
–
NHLBI NIH HHS HL44491NIDDK NIH HHS R29-DK40242
6 · The paper itself

Abstract

Erythrocyte development in mammals depends in part upon the interaction of the glycopeptide hormone erythropoietin (EPO) with cell surface receptors on committed erythroid progenitor cells. Both this factor and an EPO receptor polypeptide previously have been cloned, yet little is presently understood concerning molecular mechanisms of receptor activation and signal transduction. To identify cytosolic receptor domains necessary for signaling, we have compared the activities of a series of deletionally mutated EPO receptor constructs by their expression in interleukin 3-dependent, myeloid FDC-P1 cells. EPO-induced growth was transduced efficiently in these cells by the full-length receptor (507 amino acids), and no measurable loss in activity resulted from the deletion of up to 111 carboxyl-terminal residues. In contrast, the deletion of 44 additional residues led to a dramatic loss (86.3% +/- 7.8%; mean +/- SD) in the ability of this receptor to mediate EPO-induced growth, thus indicating that residues between Gly-352 and Met-396 constitute a functionally critical cytosolic subdomain. Interestingly, the expression of full-length EPO receptors in FDC-P1 cells also led to a selective inhibition of normal proliferative responsiveness to the alternative hematopoietic factor granulocyte-macrophage colony-stimulating factor. Moreover, this inhibition was progressively reversed in forms of the EPO receptor in which distal cytosolic residues were sequentially deleted. These results suggest that EPO receptors normally may trans-modulate components in the pathway of granulocyte-macrophage colony-stimulating factor-induced proliferation and that this down-modulation, as exerted by intact EPO receptors, may play a role in promoting erythroid commitment during myeloid blood cell development.

Indexed as

Signal TransductionAnimalsBase SequenceBlotting, NorthernBlotting, WesternCell LineChromosome DeletionClone CellsCytosolErythropoietinGranulocyte-Macrophage Colony-Stimulating FactorInterleukin-3MiceMolecular Sequence DataOligonucleotide ProbesPlasmidsErythropoietinGranulocyte-Macrophage Colony-Stimulating FactorInterleukin-3Oligonucleotide ProbesReceptors, Cell SurfaceReceptors, ErythropoietinRNA

Identifiers

PMID1711211
PMCPMC51754
OpenAlexW2070395474

What OpenQuestion holds

Textmetadata
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.