Evidence map›Paper›PMID 26903292›Full record

ArticleLife sciences2016

Effect of alpha 2,6 sialylation on integrin-mediated adhesion of breast cancer cells to fibronectin and collagen IV.

Ye Yuan, Larry Wu, Siqi Shen, Shiyong Wu, Monica M Burdick

Open access · greenAbstract read
In one paragraph

Article in Life sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Inhaled Angiopoietin-Like 4 Antisense Oligonucleotide Therapy for Lung Injury and Fibrosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
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  5. Review
  6. Article
  7. Review
  8. Reducing Sialylation Enhances Electrotaxis of Corneal Epithelial Cells.International journal of molecular sciences · 2023
    Article
  9. Review
  10. Site-specificiScience · 2021
    Article
  11. Review
  12. Altered Actin Dynamics in Cell Migration of GNE Mutant Cells.Frontiers in cell and developmental biology · 2021
    Article
  13. Altered glycosylation in cancer: A promising target for biomarkers and therapeutics.Biochimica et biophysica acta. Reviews on cancer · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. 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

5 authors at 3 institutions in 2 countries.

Ye YuanEdison Biotechnology Institute, Ohio University, Athens, OH, United States; Department of Chemistry and Biochemistry, Ohio University, Athens, OH, United States.
Larry WuDepartment of Chemical and Biomolecular Engineering, Ohio University, Athens, OH, United States.
Siqi ShenCollege of Life Sciences, Capital Normal University, Beijing, China.
Shiyong WuEdison Biotechnology Institute, Ohio University, Athens, OH, United States; Department of Chemistry and Biochemistry, Ohio University, Athens, OH, United States. Electronic address: wus1@ohio.edu.
Monica M BurdickDepartment of Chemical and Biomolecular Engineering, Ohio University, Athens, OH, United States. Electronic address: burdick@ohio.edu.
Biotechnology Institute · USOhio University · USCapital Normal University · CN

Funding

UV INDUCED AND PERK MEDIATED SIGNALING PATHWAYSR01CA086928 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WU, SHIYONG · 2000 to 2012
$2.1M
NCI NIH HHS R01 CA086928NCI NIH HHS R01CA086928
6 · The paper itself

Abstract

aimsTo determine the role of sialylation on α5β1 and α2β1 integrins in the regulation of adhesion between breast cancer cells and extracellular matrix (ECM). MAIN

methodsStatic cell adhesion assays were performed to quantify avidity of breast cancer cells to ECM. The effects of sialidases on α2,6 sialylation was assessed by flow cytometry using biotin conjugated Sambucus nigra lectin. Lectin affinity assays were used to determine expression of α2,6 sialylated integrins. Cell migration and invasion were investigated by wound healing and transwell invasion assays. KEY

findingsα2, α5 and β1 integrins had considerable α2,6 sialylation on MDA-MB-231 cells, whereas signals from MCF-7 cells were undetectable. Cleavage of α2,6 sialylation increased adhesion of MDA-MB-231 cells to ECM, while adhesion of MCF-7 cells was unaffected, consistent with the latter's lack of endogenous α2,6 sialylated surface integrins. Neither surface expression of α2β1 and α5β1 integrins, nor activated β1 integrin, changed in MDA-MB-231 cells after sialidase treatment. However, sialidase treatment did not have significant impact on migration or invasion of MDA-MB-231 cells. SIGNIFICANCE: Cell adhesion is an important early step of cancer metastasis, yet the roles of sialylation in regulating integrin-mediated breast cancer cell adhesion in comparison to migration and invasion are not well-understood. Our data suggest desialylation of α2,6-sialylated integrins increases adhesion, but not migration or invasion, of MDA-MB-231 cells to ECM without altering integrin expression. It should be considered that α2,6 sialylation may play different roles in regulating cell adhesion of different cancer cells when developing potential therapeutics targeting α2,6 sialylation.

Indexed as

Cell AdhesionCollagen Type IVFemaleFibronectinsHumansIntegrinsMCF-7 CellsNeuraminidaseCollagen Type IVFibronectinsIntegrinsNeuraminidaseBreast neoplasmsCell adhesionExtracellular matrixIntegrinsN-acetylneuraminic acid

Identifiers

PMID26903292
PMCPMC4792681
OpenAlexW2281637108

What OpenQuestion holds

Textmetadata
LicenceTDM
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.