Evidence map›Paper›PMID 25951175›Full record

ArticlePloS one2015

The Breast Cancer-Associated Glycoforms of MUC1, MUC1-Tn and sialyl-Tn, Are Expressed in COSMC Wild-Type Cells and Bind the C-Type Lectin MGL.

Richard Beatson, Gjertrud Maurstad, Gianfranco Picco, Appitha Arulappu, Julia Coleman, Hans H Wandell, Henrik Clausen, Ulla Mandel, Joyce Taylor-Papadimitriou, Marit Sletmoen and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 103 citations in OpenAlex.

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  15. Glycosylation Targeting: A Paradigm Shift in Cancer Immunotherapy.International journal of biological sciences · 2024
    Review
  16. Review
  17. Review
  18. Role of TruncatedCancers · 2023
    Review
  19. Article
  20. Review

5 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 3 countries.

Richard BeatsonBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
Gjertrud MaurstadDepartment of Physics, Norwegian University of Science and Technology, 7491, Trondheim, Norway.
Gianfranco PiccoBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
Appitha ArulappuBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
Julia ColemanBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
Hans H WandellCopenhagen Center for Glycomics, University of Copenhagen, Copenhagen, DK-2200, Denmark.
Henrik ClausenCopenhagen Center for Glycomics, University of Copenhagen, Copenhagen, DK-2200, Denmark.
Ulla MandelCopenhagen Center for Glycomics, University of Copenhagen, Copenhagen, DK-2200, Denmark.
Joyce Taylor-PapadimitriouBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
Marit SletmoenDepartment of Physics, Norwegian University of Science and Technology, 7491, Trondheim, Norway.
Joy M BurchellBreast Cancer Biology, King's College London, Guy's Hospital, London, SE1 9RT, United Kingdom.
King's College London · GBUniversity of Copenhagen · DKGuy's Hospital · GBNorwegian University of Science and Technology · NO

Funding

Department of Health
6 · The paper itself

Abstract

Aberrant glycosylation occurs in the majority of human cancers and changes in mucin-type O-glycosylation are key events that play a role in the induction of invasion and metastases. These changes generate novel cancer-specific glyco-antigens that can interact with cells of the immune system through carbohydrate binding lectins. Two glyco-epitopes that are found expressed by many carcinomas are Tn (GalNAc-Ser/Thr) and STn (NeuAcα2,6GalNAc-Ser/Thr). These glycans can be carried on many mucin-type glycoproteins including MUC1. We show that the majority of breast cancers carry Tn within the same cell and in close proximity to extended glycan T (Galβ1,3GalNAc) the addition of Gal to the GalNAc being catalysed by the T synthase. The presence of active T synthase suggests that loss of the private chaperone for T synthase, COSMC, does not explain the expression of Tn and STn in breast cancer cells. We show that MUC1 carrying both Tn or STn can bind to the C-type lectin MGL and using atomic force microscopy show that they bind to MGL with a similar dead adhesion force. Tumour associated STn is associated with poor prognosis and resistance to chemotherapy in breast carcinomas, inhibition of DC maturation, DC apoptosis and inhibition of NK activity. As engagement of MGL in the absence of TLR triggering may lead to anergy, the binding of MUC1-STn to MGL may be in part responsible for some of the characteristics of STn expressing tumours.

Indexed as

Antigens, Tumor-Associated, CarbohydrateBreast NeoplasmsCell Line, TumorFemaleHumansLectins, C-TypeMucin-1Protein BindingAntigens, Tumor-Associated, CarbohydrateLectins, C-TypeMGL lectin, humanMUC1 protein, humanMucin-1Tn antigen

Identifiers

PMID25951175
PMCPMC4423978
OpenAlexW839441936

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.