Evidence map›Paper›PMID 20049476›Full record

ArticleJournal of cancer research and clinical oncology2010

Nucleolin as cell surface receptor for tumor necrosis factor-alpha inducing protein: a carcinogenic factor of Helicobacter pylori.

Tatsuro Watanabe, Hideaki Tsuge, Takahito Imagawa, Daisuke Kise, Kazuya Hirano, Masatoshi Beppu, Atsushi Takahashi, Kensei Yamaguchi, Hirota Fujiki, Masami Suganuma

Open access · greenAbstract read
In one paragraph

Article in Journal of cancer research and clinical oncology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022
    Review
  6. Article
  7. Review
  8. Frontiers in cell and developmental biology · 2021
    Article
  9. Article
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  12. Clinical and laboratory importance of detectingPrzeglad gastroenterologiczny · 2020
    Review
  13. Article
  14. Review
  15. Article
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  18. Article
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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

10 authors at 4 institutions in 1 country.

Tatsuro WatanabeSaitama Cancer Center, Research Institute for Clinical Oncology, Kitaadachi-gun, Saitama 362-0806, Japan.
Hideaki Tsuge
Takahito Imagawa
Daisuke Kise
Kazuya Hirano
Masatoshi Beppu
Atsushi Takahashi
Kensei Yamaguchi
Hirota Fujiki
Masami Suganuma
Tokushima Bunri University · JPSaitama Cancer Center · JPTokyo University of Pharmacy and Life Sciences · JPSaitama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeTumor necrosis factor-alpha inducing protein (Tipalpha) is a unique carcinogenic factor released from Helicobacter pylori (H. pylori). Tipalpha specifically binds to cells and is incorporated into cytosol and nucleus, where it strongly induces expression of TNF-alpha and chemokine genes mediated through NF-kappaB activation, resulting in tumor development. To elucidate mechanism of action of Tipalpha, we studied a binding protein of Tipalpha in gastric epithelial cells.

methodsTipalpha binding protein was found in cell lysates of mouse gastric cancer cell line MGT-40 by FLAG-pull down assay and identified to be cell surface nucleolin by flow cytometry using anti-nucleolin antibody. Incorporation of Tipalpha into the cells was determined by Western blotting and expression of TNF-alpha gene was quantified by RT-PCR.

resultsNucleolin was co-precipitated with Tipalpha-FLAG, but not with del-Tipalpha-FLAG (an inactive mutant). After treatment with Tipalpha-FLAG, incorporated Tipalpha was co-immunoprecipitated with endogenous nucleolin using anti-nucleolin antibody. The direct binding of Tipalpha to recombinant His-tagged nucleolin fragment (284-710) was also confirmed. Although nucleolin is an abundant non-ribosomal protein of the nucleolus, we found that nucleolin is present on the cell surface of MGT-40 cells. Pretreatment with anti-nucleolin antibody enhanced Tipalpha-incorporation into the cells through nucleolin internalization. In addition, pretreatment with tunicamycin, an inhibitor of N-glycosylation, decreased the amounts of cell surface nucleolin and inhibited both internalization of Tipalpha and expression of TNF-alpha gene.

conclusionsAll the results indicate that nucleolin acts as a receptor for Tipalpha and shuttles Tipalpha from cell surface to cytosol and nuclei. These findings provide a new mechanistic insight into gastric cancer development with Tipalpha.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsBlotting, WesternCarcinogensChromatography, LiquidDown-RegulationEpithelial CellsFlow CytometryGene Expression Regulation, NeoplasticImmunoprecipitationMass SpectrometryMiceMolecular Sequence DataNF-kappa BNucleolinBacterial ProteinsCarcinogensNF-kappa BNucleolinPhosphoproteinsReceptors, Cell SurfaceRNA-Binding ProteinsTipalpha protein, Helicobacter pyloriTumor Necrosis Factor-alpha

Identifiers

PMID20049476
PMCPMC11828327
OpenAlexW1994466698

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.