Evidence map›Paper›PMID 18467504›Full record

ArticleAmerican journal of physiology. Gastrointestinal and liver physiology2008

Tumor necrosis factor inhibits ligand-stimulated EGF receptor activation through a TNF receptor 1-dependent mechanism.

Steven J McElroy, Mark R Frey, Fang Yan, Karen L Edelblum, Jeremy A Goettel, Sutha John, D Brent Polk

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Gastrointestinal and liver physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

23 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. TPN-associated intestinal epithelial cell atrophy is modulated by TLR4/EGF signaling pathways.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

7 authors at 1 institution in 1 country.

Steven J McElroyDept. of Pediatrics, Div. of Pediatric Gastroenterology, Hepatology, and Nutrition, 2215 Garland Ave., 1035 MRB IV, Nashville TN, 37232-0696, USA.
Mark R Frey
Fang Yan
Karen L Edelblum
Jeremy A Goettel
Sutha John
D Brent Polk
Baylor Medical Center at Garland · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
CYTOKINE REGULATION OF INTESTINAL EPITHELIAL RESTITUTIONR01DK056008 · NIDDK · VANDERBILT UNIVERSITY · PI POLK, D BRENT · 1999 to 2020
$6.8M
Training Program in Pediatric Cardiopulmonary ResearchT32HL007256 · NHLBI · VANDERBILT UNIVERSITY · PI BALDWIN, H SCOTT · 1985 to 2006
$906k
NHLBI NIH HHS 2T32HL07256-26NIDDK NIH HHS 2P30 DK058404-06NIDDK NIH HHS 5R01DK056008-09
6 · The paper itself

Abstract

Tumor necrosis factor (TNF) and epidermal growth factor (EGF) are key regulators in the intricate balance maintaining intestinal homeostasis. Previous work from our laboratory shows that TNF attenuates ligand-driven EGF receptor (EGFR) phosphorylation in intestinal epithelial cells. To identify the mechanisms underlying this effect, we examined EGFR phosphorylation in cells lacking individual TNF receptors. TNF attenuated EGF-stimulated EGFR phosphorylation in wild-type and TNFR2(-/-), but not TNFR1(-/-), mouse colon epithelial (MCE) cells. Reexpression of wild-type TNFR1 in TNFR1(-/-) MCE cells rescued TNF-induced EGFR inhibition, but expression of TNFR1 deletion mutant constructs lacking the death domain (DD) of TNFR1 did not, implicating this domain in EGFR downregulation. Blockade of p38 MAPK, but not MEK, activation of ERK rescued EGF-stimulated phosphorylation in the presence of TNF, consistent with the ability of TNFR1 to stimulate p38 phosphorylation. TNF promoted p38-dependent EGFR internalization in MCE cells, suggesting that desensitization is achieved by reducing receptor accessible to ligand. Taken together, these data indicate that TNF activates TNFR1 by DD- and p38-dependent mechanisms to promote EGFR internalization, with potential impact on EGF-induced proliferation and migration key processes that promote healing in inflammatory intestinal diseases.

Indexed as

AnimalsCells, CulturedEpidermal Growth FactorErbB ReceptorsMicep38 Mitogen-Activated Protein KinasesPhosphorylationReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alphaEpidermal Growth FactorErbB Receptorsp38 Mitogen-Activated Protein KinasesReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alpha

Identifiers

PMID18467504
PMCPMC2519857
OpenAlexW2162976850

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.