Evidence map›Paper›PMID 23814067›Full record

ArticleThe Journal of biological chemistry2013

Trimeric Tn antigen on syndecan 1 produced by ppGalNAc-T13 enhances cancer metastasis via a complex formation with integrin α5β1 and matrix metalloproteinase 9.

Yasuyuki Matsumoto, Qing Zhang, Kaoru Akita, Hiroshi Nakada, Kazunori Hamamura, Akiko Tsuchida, Tetsuya Okajima, Keiko Furukawa, Takeshi Urano, Koichi Furukawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. GALNT1 emerges as a potential therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2026
    Article
  4. GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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  13. Article
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  15. Article
  16. PolypeptideOncoTargets and therapy · 2017
    Article
  17. Article
  18. Article
  19. Review
  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

10 authors at 5 institutions in 1 country.

Yasuyuki MatsumotoDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Qing Zhang
Kaoru Akita
Hiroshi Nakada
Kazunori Hamamura
Akiko Tsuchida
Tetsuya Okajima
Keiko Furukawa
Takeshi Urano
Koichi Furukawa
Nagoya University · JPKyoto Sangyo University · JPChubu University · JPNoguchi Institute · JPShimane University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We demonstrated previously that ppGalNAc-T13 (T13), identified as an up-regulated gene with increased metastasis in a DNA microarray, generated trimeric Tn (tTn) antigen (GalNAcα1-Ser/Thr)3 on Syndecan 1 in highly metastatic sublines of Lewis lung cancer. However, it is not known how tTn antigen regulates cancer metastasis. Here, we analyzed the roles of tTn antigen in cancer properties. tTn antigen on Syndecan 1 increased cell adhesion to fibronectin in an integrin-dependent manner. Furthermore, cell adhesion to fibronectin induced phosphorylation of focal adhesion kinase and paxillin in T13-transfectant cells. In the search of Syndecan 1-interacting molecules, it was demonstrated that tTn antigen-carrying Syndecan 1 interacted with integrin α5β1 and matrix metalloproteinase 9 and that these molecules shifted to a glycolipid-enriched microdomain/rafts along with increased metastatic potential in T13-transfectant cells. We also identified a tTn substitution site on Syndecan 1, demonstrating that tTn on Syndecan 1 is essential for the interaction with integrin α5β1 as well as for the reaction with mAb MLS128. These data suggest that high expression of the ppGalNAc-T13 gene generates tTn antigen on Syndecan 1 under reduced expression of GM1, leading to enhanced invasion and metastasis via the formation of a molecular complex consisting of integrin α5β1, Syndecan 1, and MMP-9 in the glycolipid-enriched microdomain/rafts.

Indexed as

Protein MultimerizationAnimalsAntigens, Tumor-Associated, CarbohydrateBase SequenceCarcinoma, Lewis LungCell AdhesionFibronectinsFocal Adhesion Protein-Tyrosine KinasesGene Knockdown TechniquesIntegrin alpha5beta1Matrix Metalloproteinase 9Membrane MicrodomainsMiceModels, BiologicalMolecular Sequence DataN-AcetylgalactosaminyltransferasesAntigens, Tumor-Associated, CarbohydrateFibronectinsFocal Adhesion Protein-Tyrosine KinasesIntegrin alpha5beta1Matrix Metalloproteinase 9N-AcetylgalactosaminyltransferasesPaxillinPhosphotyrosinePolypeptide N-acetylgalactosaminyltransferaseSyndecan-1Tn antigenGlycolipidsGlycosylationIntegrinsLung CancerMetastasisO-glycansTn Antigen

Identifiers

PMID23814067
PMCPMC3745370
OpenAlexW2119911439

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.