Evidence map›Paper›PMID 25167227›Full record

ArticleBritish journal of cancer2014

The glycosphingolipid P₁ is an ovarian cancer-associated carbohydrate antigen involved in migration.

F Jacob, M Anugraham, T Pochechueva, B W C Tse, S Alam, R Guertler, N V Bovin, A Fedier, N F Hacker, M E Huflejt and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in British journal of cancer, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

24 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
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  4. Serum antibody screening using glycan arrays.Chemical Society reviews · 2024
    Review
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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

12 authors at 3 institutions in 2 countries.

F Jacob1] Gynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland [2] Ovarian Cancer Group, Adult Cancer Program, Lowy Cancer Research Centre, University of New South Wales, Prince of Wales Clinical School, Building C25 Kensington Campus, Sydney, NSW 2052, Australia.
M AnugrahamDepartment of Chemistry and Biomolecular Sciences, Biomolecular Frontiers Research Centre, Faculty of Science, Macquarie University, Balaclava Road, North Ryde, Sydney, NSW 2109, Australia.
T PochechuevaGynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland.
B W C Tse1] Ovarian Cancer Group, Adult Cancer Program, Lowy Cancer Research Centre, University of New South Wales, Prince of Wales Clinical School, Building C25 Kensington Campus, Sydney, NSW 2052, Australia [2] Australian Prostate Cancer Research Centre Queensland, Institute of Health and Biomedical Innovation, Queensland University of Technology, Translational Research Institute, Brisbane, QLD 4102, Australia.
S AlamGynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland.
R Guertler1] Gynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland [2] Ovarian Cancer Group, Adult Cancer Program, Lowy Cancer Research Centre, University of New South Wales, Prince of Wales Clinical School, Building C25 Kensington Campus, Sydney, NSW 2052, Australia.
N V BovinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya, 16/10, Moscow 117997, Russian Federation.
A FedierGynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland.
N F HackerGynaecological Cancer Centre, Royal Hospital for Women, School of Women's and Children's Health, Barker Street, Randwick, NSW 2031, Australia.
M E HuflejtDivision of Thoracic Surgery and Thoracic Oncology, Department of Cardiothoracic Surgery, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
N PackerDepartment of Chemistry and Biomolecular Sciences, Biomolecular Frontiers Research Centre, Faculty of Science, Macquarie University, Balaclava Road, North Ryde, Sydney, NSW 2109, Australia.
V A Heinzelmann-Schwarz1] Gynecological Research Group, Department of Biomedicine, University Hospital Basel, University of Basel, Hebelstrasse 20, Basel 4031, Switzerland [2] Ovarian Cancer Group, Adult Cancer Program, Lowy Cancer Research Centre, University of New South Wales, Prince of Wales Clinical School, Building C25 Kensington Campus, Sydney, NSW 2052, Australia [3] Gynaecological Cancer Centre, Royal Hospital for Women, School of Women's and Children's Health, Barker Street, Randwick, NSW 2031, Australia.
University of Basel · CHNew York University · USUniversity Hospital of Basel · CH

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Cheongeun Oh · 1985 to 2026
$83.1M
NCI NIH HHS P30 CA016087
6 · The paper itself

Abstract

backgroundThe level of plasma-derived naturally circulating anti-glycan antibodies (AGA) to P1 trisaccharide has previously been shown to significantly discriminate between ovarian cancer patients and healthy women. Here we aim to identify the Ig class that causes this discrimination, to identify on cancer cells the corresponding P1 antigen recognised by circulating anti-P1 antibodies and to shed light into the possible function of this glycosphingolipid.

methodsAn independent Australian cohort was assessed for the presence of anti-P1 IgG and IgM class antibodies using suspension array. Monoclonal and human derived anti-glycan antibodies were verified using three independent glycan-based immunoassays and flow cytometry-based inhibition assay. The P1 antigen was detected by LC-MS/MS and flow cytometry. FACS-sorted cell lines were studied on the cellular migration by colorimetric assay and real-time measurement using xCELLigence system.

resultsHere we show in a second independent cohort (n=155) that the discrimination of cancer patients is mediated by the IgM class of anti-P1 antibodies (P=0.0002). The presence of corresponding antigen P1 and structurally related epitopes in fresh tissue specimens and cultured cancer cells is demonstrated. We further link the antibody and antigen (P1) by showing that human naturally circulating and affinity-purified anti-P1 IgM isolated from patients ascites can bind to naturally expressed P1 on the cell surface of ovarian cancer cells. Cell-sorted IGROV1 was used to obtain two study subpopulations (P1-high, 66.1%; and P1-low, 33.3%) and observed that cells expressing high P1-levels migrate significantly faster than those with low P1-levels.

conclusionsThis is the first report showing that P1 antigen, known to be expressed on erythrocytes only, is also present on ovarian cancer cells. This suggests that P1 is a novel tumour-associated carbohydrate antigen recognised by the immune system in patients and may have a role in cell migration. The clinical value of our data may be both diagnostic and prognostic; patients with low anti-P1 IgM antibodies present with a more aggressive phenotype and earlier relapse.

Indexed as

Antibodies, NeoplasmAntigens, NeoplasmCell Line, TumorChromatography, AffinityFemaleFlow CytometryGlycosphingolipidsHumansNeoplasm MetastasisOvarian NeoplasmsAntibodies, NeoplasmAntigens, NeoplasmGlycosphingolipids

Identifiers

PMID25167227
PMCPMC4200095
OpenAlexW1522617432

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.