Evidence map›Paper›PMID 22992780›Full record

ArticleInternational journal of molecular medicine2012

Polypeptide N-acetylgalactosaminyltransferase 2 regulates cellular metastasis-associated behavior in gastric cancer.

Dong Hua, Li Shen, Lan Xu, Zhi Jiang, Yinghui Zhou, Aihuan Yue, Shitao Zou, Zhihong Cheng, Shiliang Wu

Open access · hybridAbstract read
In one paragraph

Article in International journal of molecular medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Anti-Cancer Potential of Afzelin towards AGS Gastric Cancer Cells.Pharmaceuticals (Basel, Switzerland) · 2021
    Article
  5. C1GALT1 in health and disease.Oncology letters · 2021
    Review
  6. High Expression of N-Acetylgalactosaminyl-transferase 1 (GALNT1) Associated with Invasion, Metastasis, and Proliferation in Osteosarcoma.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. 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

9 authors at 2 institutions in 1 country.

Dong HuaFourth Affiliated Hospital of Soochow University, Wuxi, Jiangsu 214062, P.R. China.
Li Shen
Lan Xu
Zhi Jiang
Yinghui Zhou
Aihuan Yue
Shitao Zou
Zhihong Cheng
Shiliang Wu
Soochow University · CNThe Fourth Affiliated Hospital of Soochow University (Suzhou Dushu Lake Hospital)

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aberrant glycosylation of cell surface glycoprotein due to specific alterations of glycosyltransferase activity is usually associated with invasion and metastasis of cancer, particularly of gastric carcinomas. Polypeptide N-acetylgalactosaminyltransferase 2 (ppGalNAc-T2), which catalyzes initiation of mucin-type O-glycosylation, is also involved in tumor migration and invasion. However, a comprehensive understanding of how ppGalNAc-T2 correlates with the metastasic potential of human gastric cancer is not currently available. In the present study, ppGalNAc-T2 was detected in a variety of human poorly differentiated tumor cells, and expression appeared to be higher in SGC7901 gastric cancer cells. In addition, we investigated the potential effects of ppGalNAc-T2 on growth and metastasis-associated behavior in SGC7901 cells after stable transfection with ppGalNAc-T2 sense and antisense vectors. We found that cell proliferation, adhesion and invasion were decreased in ppGalNAc-T2 overexpressed cells but increased in ppGalNAc-T2 downregulated cells. Therefore, we attempted to clarify the mechanisms underlying the anti-metastatic activities of ppGalNAc-T2. Further investigation indicated that overexpression of ppGalNAc-T2 is involved in the inhibition of matrix metalloproteinase (MMP)-2 expression at both the protein and mRNA levels, which may be associated with ppGalNAc-T2 suppressing the expression of transforming growth factor (TGF)-β1. However, it did not exhibit any apparent correlation with MMP-14 expression levels. Our data show the effect of ppGalNAc-T2 on proliferation, adhesion or invasion of SGC7901 gastric cancer cells, suggesting that ppGalNAc-T2 may exert anti-proliferative and anti-metastatic activity through the decrease of MMP-2 and TGF-β1. These results indicate that ppGalNAc‑T2 may be used as a novel therapeutic target for human gastric cancer treatment.

Indexed as

Cell MovementCell AdhesionCell Line, TumorCell ProliferationCell SurvivalGene ExpressionGene Knockdown TechniquesHumansMatrix Metalloproteinase 14Matrix Metalloproteinase 2N-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseStomach NeoplasmsTransforming Growth Factor beta1Matrix Metalloproteinase 14Matrix Metalloproteinase 2MMP14 protein, humanMMP2 protein, humanN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseTransforming Growth Factor beta1

Identifiers

PMID22992780
PMCPMC4042861
OpenAlexW2091727244

What OpenQuestion holds

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LicenceCC BY
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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.