Evidence map›Paper›PMID 19218444›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Identification of mRNA splicing factors as the endothelial receptor for carbohydrate-dependent lung colonization of cancer cells.

Shingo Hatakeyama, Kazuhiro Sugihara, Jun Nakayama, Tomoya O Akama, Shuk-Man Annie Wong, Hiroto Kawashima, Jianing Zhang, David F Smith, Chikara Ohyama, Minoru Fukuda and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 9% 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, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
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  13. Targeted drug delivery to tumor vasculature by a carbohydrate mimetic peptide.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  16. Dynamics of galectin-3 in the nucleus and cytoplasm.Biochimica et biophysica acta · 2010
    Review
  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

11 authors at 6 institutions in 3 countries.

Shingo HatakeyamaTumor Microenvironment Program, Cancer Research Center, Burnham Institute for Medical Research, La Jolla, CA 92037, USA.
Kazuhiro Sugihara
Jun Nakayama
Tomoya O Akama
Shuk-Man Annie Wong
Hiroto Kawashima
Jianing Zhang
David F Smith
Chikara Ohyama
Minoru Fukuda
Michiko N Fukuda
Sanford Burnham Prebys Medical Discovery Institute · USDalian Medical University · CNEmory University · USHamamatsu University School of Medicine · JPHirosaki University · JPShinshu University · JP

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2001 to 2010
$80.3M
THE A(1,3)FUCOSYLTRANSFERASE GENES AND SELECTIN LIGAND EXPRESSIONP01CA071932 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LOWE, JOHN B · 1996 to 2012
$15.5M
NCI NIH HHS P01 CA071932NCI NIH HHS P01CA071932NIGMS NIH HHS GM62116NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Cell surfaces of epithelial cancer are covered by complex carbohydrates, whose structures function in malignancy and metastasis. However, the mechanism underlying carbohydrate-dependent cancer metastasis has not been defined. Previously, we identified a carbohydrate-mimicry peptide designated I-peptide, which inhibits carbohydrate-dependent lung colonization of sialyl Lewis X-expressing B16-FTIII-M cells in E/P-selectin doubly-deficient mice. We hypothesized that lung endothelial cells express an unknown carbohydrate receptor, designated as I-peptide receptor (IPR), responsible for lung colonization of B16-FTIII-M cells. Here, we visualized IPR by in vivo biotinylation, which revealed that the major IPR is a group of 35-kDa proteins. IPR proteins isolated by I-peptide affinity chromatography were identified by proteomics as Ser/Arg-rich alternative pre-mRNA splicing factors or Sfrs1, Sfrs2, Sfrs5, and Sfrs7 gene products. Bacterially expressed Sfrs1 protein bound to B16-FTIII-M cells but not to parental B16 cells. Recombinant Sfrs1 protein bound to a series of fucosylated oligosaccharides in glycan array and plate-binding assays. When anti-Sfrs antibodies were injected intravenously into mice, antibodies labeled a subset of lung capillaries. Anti-Sfrs antibodies inhibited homing of I-peptide-displaying phage to the lung colonization of B16-FTIII-M cells in vivo in the mouse. These results strongly suggest that Sfrs proteins are responsible for fucosylated carbohydrate-dependent lung metastasis of epithelial cancers.

Indexed as

Carbohydrate MetabolismAnimalsAntibodiesCell Line, TumorCell MembraneEndothelial CellsLung NeoplasmsMiceMice, Inbred C57BLNuclear ProteinsAntibodiesNuclear Proteins

Identifiers

PMID19218444
PMCPMC2642669
OpenAlexW1978428811

What OpenQuestion holds

Textmetadata
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.