Evidence map›Paper›PMID 2165128›Full record

ArticleThe Journal of experimental medicine1990

Shedding of tumor necrosis factor receptors by activated human neutrophils.

F Porteu, C Nathan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
13.8field-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

99 citing papers in PubMed, 437 citations in OpenAlex.

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  15. Characterization of TNF receptor subtype expression and signaling on pulmonary endothelial cells in mice.American journal of physiology. Lung cellular and molecular physiology · 2011
    Article
  16. Article
  17. Review
  18. Article
  19. Molecular and cellular mechanisms of ectodomain shedding.Anatomical record (Hoboken, N.J. : 2007) · 2010
    Review
  20. Elevated endotoxin levels in non-alcoholic fatty liver disease.Journal of inflammation (London, England) · 2010
    Article

39 more citing papers are in PubMed but not listed here.

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.

F PorteuDepartment of Medicine, Cornell University Medical College, New York, New York 10021.
C Nathan
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The capacity of human neutrophils (PMN) to bind tumor necrosis factor (TNF) was rapidly lost when the cells were incubated in suspension with agents that can stimulate their migratory and secretory responses. Both physiological (poly)peptides (FMLP, C5a, CSF-GM) and pharmacologic agonists (PMN, calcium ionophore A23187) induced the loss of TNF receptors (TNF-R) from the cell surface. Half-maximal loss in TNF-R ensued after only approximately 2 min with 10(-7) M FMLP at 37 degrees C, and required only 10(-9) M FMLP during a 30-min exposure. However, there were no such changes even with prolonged exposure of PMN to FMLP at 4 degrees or 16 degrees C. Scatchard analysis revealed loss of TNF-binding sites without change in their affinity (Kd approximately 0.4 nM) as measured at incompletely modulating concentrations of FMLP, C5a, PMA, or A23187. The binding of anti-TNF-R mAbs to PMN decreased in parallel, providing independent evidence for the loss of TNF-R from the cell surface. At the same time, soluble TNF-R appeared in the medium of stimulated PMN. This inference was based on the PMN- and FMLP-dependent generation of a nonsedimentable activity that could inhibit the binding of TNF to fresh human PMN or to mouse macrophages, and the ability of mAbs specific for human TNF-R to abolish inhibition by PMN-conditioned medium of binding of TNF to mouse macrophages. Soluble TNF-R activity was associated with a protein of Mr approximately 28,000 by ligand blot analysis of cell-free supernatants of FMLP-treated PMN. Thus, some portion of the FMLP-induced loss of TNF-R from human PMN is due to shedding of TNF-R. Shedding was unaffected by inhibitors of serine and thiol proteases and could not be induced with phosphatidylinositol-specific phospholipase C. Loss of TNF-R from PMN first stimulated by other agents may decrease their responsiveness to TNF. TNF-R shed by PMN may be one source of the TNF-binding proteins found in body fluids, and may blunt the actions of the cytokine on other cells.

Indexed as

Biological FactorsChemotactic FactorsCytokinesDown-RegulationGrowth SubstancesHumansKineticsNeutrophilsN-Formylmethionine Leucyl-PhenylalanineProtease InhibitorsReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorRecombinant ProteinsTumor Necrosis Factor-alphaBiological FactorsChemotactic FactorsCytokinesGrowth SubstancesN-Formylmethionine Leucyl-PhenylalanineProtease InhibitorsReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorRecombinant ProteinsTumor Necrosis Factor-alpha

Identifiers

PMID2165128
PMCPMC2188336
OpenAlexW2182204751

What OpenQuestion holds

Textmetadata
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.