Evidence map›Paper›PMID 20705048›Full record

ArticleAnalytical biochemistry2011

A lectin affinity workflow targeting glycosite-specific, cancer-related carbohydrate structures in trypsin-digested human plasma.

Penelope M Drake, Birgit Schilling, Richard K Niles, Miles Braten, Eric Johansen, Haichuan Liu, Michael Lerch, Dylan J Sorensen, Bensheng Li, Simon Allen and 5 more

Abstract read
In one paragraph

Article in Analytical biochemistry, 2011. 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
3.1field-weighted citation impact, top 8% 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, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Chemical Glycoproteomics.Chemical reviews · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. N- and O-glycosylation in the murine synaptosome.Molecular & cellular proteomics : MCP · 2013
    Article
  16. Glycopeptide analysis, recent developments and applications.Molecular & cellular proteomics : MCP · 2013
    Review
  17. 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

15 authors at 3 institutions in 1 country.

Penelope M DrakeDepartment of Obstetrics, Gynecology and Reproductive Sciences, University of California San Francisco, 94143, USA.
Birgit Schilling
Richard K Niles
Miles Braten
Eric Johansen
Haichuan Liu
Michael Lerch
Dylan J Sorensen
Bensheng Li
Simon Allen
Steven C Hall
H Ewa Witkowska
Fred E Regnier
Bradford W Gibson
Susan J Fisher
University of California, San Francisco · USBuck Institute for Research on Aging · USPurdue University West Lafayette · US

Funding

Targeted and global proteomic strategies for early breast cancer detectionU24CA126477 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FISHER, SUSAN J. · 2006 to 2011
$8.7M
QSTAR Elite Quadrupole-o-TOF LC/MS/MS SystemS10RR024615 · NCRR · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2007 to 2007
$466k
NCI NIH HHS U24 CA126477NCRR NIH HHS S10 RR024615
6 · The paper itself

Abstract

Glycans are cell-type-specific, posttranslational protein modifications that are modulated during developmental and disease processes. As such, glycoproteins are attractive biomarker candidates. Here, we describe a mass spectrometry-based workflow that incorporates lectin affinity chromatography to enrich for proteins that carry specific glycan structures. As increases in sialylation and fucosylation are prominent among cancer-associated modifications, we focused on Sambucus nigra agglutinin (SNA) and Aleuria aurantia lectin (AAL), lectins which bind sialic acid- and fucose-containing structures, respectively. Fucosylated and sialylated glycopeptides from human lactoferrin served as positive controls, and high-mannose structures from yeast invertase served as negative controls. The standards were spiked into Multiple Affinity Removal System (MARS) 14-depleted, trypsin-digested human plasma from healthy donors. Samples were loaded onto lectin columns, separated by HPLC into flow-through and bound fractions, and treated with peptide: N-glycosidase F to remove N-linked glycans. The deglycosylated peptide fractions were interrogated by ESI HPLC-MS/MS. We identified a total of 122 human plasma glycoproteins containing 247 unique glycosites. Importantly, several of the observed glycoproteins (e.g., cadherin 5 and neutrophil gelatinase-associated lipocalin) typically circulate in plasma at low nanogram per milliliter levels. Together, these results provide mass spectrometry-based evidence of the utility of incorporating lectin-separation platforms into cancer biomarker discovery pipelines.

Indexed as

Biomarkers, TumorChromatography, AffinityChromatography, High Pressure LiquidDatabases, FactualFemaleGlycopeptidesGlycoproteinsHumansLectinsMaleNeoplasmsPolysaccharidesProtein BindingSpectrometry, Mass, Electrospray IonizationTrypsinBiomarkers, TumorGlycopeptidesGlycoproteinslectin, Aleuria aurantiaLectinsPolysaccharidesTrypsin

Identifiers

PMID20705048
PMCPMC3205961
OpenAlexW2018249974

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.