Evidence map›Paper›PMID 18754874›Full record

ArticleCancer science2008

N-Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor.

Kazuko Matsumoto, Hideyuki Yokote, Tokuzo Arao, Mari Maegawa, Kaoru Tanaka, Yoshihiko Fujita, Chikako Shimizu, Toshiaki Hanafusa, Yasuhiro Fujiwara, Kazuto Nishio

Open access · bronzeAbstract read
In one paragraph

Article in Cancer science, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

43 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Core fucosylation and its roles in gastrointestinal glycoimmunology.World journal of gastrointestinal oncology · 2023
    Review
  10. The Association of the Polymorphisms in theInternational journal of molecular sciences · 2023
    Article
  11. Review
  12. Aberrant Protein Glycosylation in Brain Cancers, with Emphasis on Glioblastoma.Advances in experimental medicine and biology · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer.International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. Review
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 3 institutions in 2 countries.

Kazuko MatsumotoDepartment of Genome Biology, Kinki University School of Medicine, 377-2 Ohno-Higashi, Osaka-Sayama, Osaka, Japan.
Hideyuki Yokote
Tokuzo Arao
Mari Maegawa
Kaoru Tanaka
Yoshihiko Fujita
Chikako Shimizu
Toshiaki Hanafusa
Yasuhiro Fujiwara
Kazuto Nishio
Kindai University · JPNational Cancer Center · USOsaka Medical and Pharmaceutical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycosylation of cell surface proteins is important for cancer biology processes such as cellular proliferation or metastasis. alpha1,6-Fucosyltransferase (FUT8) transfers a fucose residue to n-linked oligosaccharides on glycoproteins. Herein, we study the effect of fucosylation on epidermal growth factor receptor (EGFR) activity and sensitivity to an EGFR-specific tyrosine kinase inhibitor (EGFR-TKI). The increased fucosylation of EGFR significantly promoted EGF-mediated cellular growth, and the decreased fucosylation by stable FUT8 knockdown weakened the growth response in HEK293 cells. The overexpression of FUT8 cells were more sensitive than the control cells to the EGFR-TKI gefitinib, and FUT8 knockdown decreased the sensitivity to gefitinib. Finally, to examine the effects in a human cancer cell line, we constructed stable FUT8 knockdown A549 cells, and found that these cells also decreased EGF-mediated cellular growth and were less sensitive than the control cells to gefitinib. In conclusion, we demonstrated that the modification of EGFR fucosylation affected EGF-mediated cellular growth and sensitivity to gefitinib. Our results provide a novel insight into how the glycosylation status of a receptor may affect the sensitivity of the cell to molecular target agents.

Indexed as

ErbB ReceptorsFucosyltransferasesGefitinibGlycosylationHumansPolysaccharidesProtein Kinase InhibitorsQuinazolinesErbB ReceptorsFucosyltransferasesGefitinibGlycoprotein 6-alpha-L-fucosyltransferasePolysaccharidesProtein Kinase InhibitorsQuinazolines

Identifiers

PMID18754874
PMCPMC11160090
OpenAlexW1976894206

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.