Evidence map›Paper›PMID 19433864›Full record

ArticleGlycobiology2009

Targeted glycoproteomic identification of cancer cell glycosylation.

Alex S Powlesland, Paul G Hitchen, Simon Parry, Sarah A Graham, Maria Marcela Barrio, Maria Teresa Elola, José Mordoh, Anne Dell, Kurt Drickamer, Maureen E Taylor

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 69 citations in OpenAlex.

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  14. Marine lectins and their medicinal applications.Applied microbiology and biotechnology · 2015
    Review
  15. Article
  16. Article
  17. Snake venom galactoside-binding lectins: a structural and functional overview.The journal of venomous animals and toxins including tropical diseases · 2015
    Article
  18. Article
  19. Article
  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 2 institutions in 2 countries.

Alex S PowleslandDivision of Molecular Biosciences, Department of Life Sciences, Imperial College, London, UK.
Paul G Hitchen
Simon Parry
Sarah A Graham
Maria Marcela Barrio
Maria Teresa Elola
José Mordoh
Anne Dell
Kurt Drickamer
Maureen E Taylor
Imperial College London · GBConsejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2001 to 2010
$80.3M
Biotechnology and Biological Sciences Research CouncilNIGMS NIH HHS GM62116Wellcome Trust 075565
6 · The paper itself

Abstract

GalMBP is a fragment of serum mannose-binding protein that has been modified to create a probe for galactose-containing ligands. Glycan array screening demonstrated that the carbohydrate-recognition domain of GalMBP selectively binds common groups of tumor-associated glycans, including Lewis-type structures and T antigen, suggesting that engineered glycan-binding proteins such as GalMBP represent novel tools for the characterization of glycoproteins bearing tumor-associated glycans. Blotting of cell extracts and membranes from MCF7 breast cancer cells with radiolabeled GalMBP was used to demonstrate that it binds to a selected set of high molecular weight glycoproteins that could be purified from MCF7 cells on an affinity column constructed with GalMBP. Proteomic and glycomic analysis of these glycoproteins by mass spectrometry showed that they are forms of CD98hc that bear glycans displaying heavily fucosylated termini, including Lewis(x) and Lewis(y) structures. The pool of ligands was found to include the target ligands for anti-CD15 antibodies, which are commonly used to detect Lewis(x) antigen on tumors, and for the endothelial scavenger receptor C-type lectin, which may be involved in tumor metastasis through interactions with this antigen. A survey of additional breast cancer cell lines reveals that there is wide variation in the types of glycosylation that lead to binding of GalMBP. Higher levels of binding are associated either with the presence of outer-arm fucosylated structures carried on a variety of different cell surface glycoproteins or with the presence of high levels of the mucin MUC1 bearing T antigen.

Indexed as

Breast NeoplasmsCell Line, TumorFusion Regulatory Protein-1GalactoseGlycomicsGlycosylationHumansLigandsMannose-Binding LectinMicroarray AnalysisMucin-1PolysaccharidesProtein BindingProtein Structure, TertiaryProteomicsFusion Regulatory Protein-1GalactoseLigandsMannose-Binding LectinMucin-1Polysaccharides

Identifiers

PMID19433864
PMCPMC2704901
OpenAlexW2137471638

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.