Evidence map›Paper›PMID 16241905›Full record

ArticleThe Biochemical journal2006

Plasma-membrane-associated sialidase (NEU3) differentially regulates integrin-mediated cell proliferation through laminin- and fibronectin-derived signalling.

Kengo Kato, Kiyoto Shiga, Kazunori Yamaguchi, Keiko Hata, Toshimitsu Kobayashi, Kaoru Miyazaki, Shigeru Saijo, Taeko Miyagi

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2006. 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
3.1field-weighted citation impact, top 9% 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, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. The extracellular sialidase NEU3 primes neutrophils.Journal of leukocyte biology · 2022
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Attenuated pulmonary fibrosis in sialidase-3 knockout (American journal of physiology. Lung cellular and molecular physiology · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Axotomy-induced ganglioside processing: a mediator of axon regeneration restricted to the PNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  15. Human airway epithelia express catalytically active NEU3 sialidase.American journal of physiology. Lung cellular and molecular physiology · 2014
    Article
  16. Neu3 sialidase-mediated ganglioside conversion is necessary for axon regeneration and is blocked in CNS axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  17. Review
  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

8 authors at 4 institutions in 1 country.

Kengo KatoDivision of Biochemistry, Miyagi Cancer Center Research Institute, Natori 981-1293, Japan.
Kiyoto Shiga
Kazunori Yamaguchi
Keiko Hata
Toshimitsu Kobayashi
Kaoru Miyazaki
Shigeru Saijo
Taeko Miyagi
Japan Science and Technology Agency · JPMiyagi Prefectural Hospital Organization · JPTohoku University · JPKihara Institute for Biological Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have found previously that human plasma-membrane-associated sialidase (NEU3), a key glycosidase for ganglioside degradation, was markedly up-regulated in human colon cancers, with an involvement in suppression of apoptosis. To elucidate the molecular mechanisms underlying increased NEU3 expression, in the present study we investigated its role in cell adhesion of human colon cancer cells. DLD-1 cells transfected with NEU3 exhibited increased adhesion to laminins and consequent cell proliferation, but decreased cell adhesion to fibronectin and collagens I and IV, compared with control cells. When triggered by laminins, NEU3 clearly stimulated phosphorylation of FAK (focal adhesion kinase) and ERK (extracellular-signal-regulated kinase), whereas there was no activation on fibronectin. NEU3 markedly enhanced tyrosine phosphorylation of integrin beta4 with recruitment of Shc and Grb-2 only on laminin-5, and NEU3 was co-immunoprecipitated by an anti-(integrin beta4) antibody, suggesting that association of NEU3 with integrin beta4 might facilitate promotion of the integrin-derived signalling on laminin-5. In addition, the promotion of phosphorylation of integrin beta1 and ILK (integrin-linked kinase) was also observed on laminins. G(M3) depletion as the result of NEU3 overexpression, assessed by TLC, appeared to be one of the causes of the increased adhesion on laminins and, in contrast, of the decreased adhesion on fibronectin - NEU3 probably having bimodal effects. These results indicate that NEU3 differentially regulates cell proliferation through integrin-mediated signalling depending on the extracellular matrix and, on laminins, NEU3 did indeed activate molecules often up-regulated in carcinogenesis, which may cause an acceleration of the malignant phenotype in cancer cells.

Indexed as

Signal TransductionCell AdhesionCell Line, TumorCell MembraneCell ProliferationFibronectinsHumansIntegrinsLamininNeuraminidaseFibronectinsIntegrinsLamininNeu3 protein, humanNeuraminidase

Identifiers

PMID16241905
PMCPMC1383714
OpenAlexW1999842850

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.