Evidence map›Paper›PMID 21513341›Full record

ArticleAnalytical chemistry2011

A proteomics platform combining depletion, multi-lectin affinity chromatography (M-LAC), and isoelectric focusing to study the breast cancer proteome.

Zhi Zeng, Marina Hincapie, Sharon J Pitteri, Samir Hanash, Joost Schalkwijk, Jason M Hogan, Hong Wang, William S Hancock

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.9field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 135 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  5. HBFP: a new repository for human body fluid proteome.Database : the journal of biological databases and curation · 2021
    Article
  6. Putting the pieces together: mapping the O-glycoproteome.Current opinion in biotechnology · 2021
    Review
  7. Review
  8. Article
  9. Review
  10. Affinity chromatography: A review of trends and developments over the past 50 years.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Review
  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

8 authors at 4 institutions in 3 countries.

Zhi ZengDepartment of Chemistry and Chemical Biology, Barnett Institute, Northeastern University, Boston, Massachusetts, USA.
Marina Hincapie
Sharon J Pitteri
Samir Hanash
Joost Schalkwijk
Jason M Hogan
Hong Wang
William S Hancock
Fred Hutch Cancer Center · USNortheastern University · USRadboud University Nijmegen · NLYonsei University · KR

Funding

Glycan Markers for the Early Detection of Breast CancerU01CA128427 · NCI · NORTHEASTERN UNIVERSITY · PI HANCOCK, WILLIAM S · 2007 to 2011
$1.6M
NCI NIH HHS U01 CA128427NCI NIH HHS U01-CA128427
6 · The paper itself

Abstract

The discovery of breast cancer associated plasma/serum biomarkers is important for early diagnosis, disease mechanism elucidation, and determination of treatment strategy for the disease. In this study of serum samples, a multidimensional fractionation platform combined with mass spectrometric analysis were used to achieve the identification of medium to lower abundance proteins, as well as to simultaneously detect glycan and abundance changes. Immuno-affinity depletion and multi-lectin chromatography (M-LAC) were integrated into an automated HPLC platform to remove high abundance protein and fractionate glycoproteins. The collected glycoproteomes were then subjected to isoelectric focusing (IEF) separation by a digital ProteomeChip (dPC), followed by in-gel digestion and LC-MS analysis using an Orbitrap mass spectrometer. As a result, the total number of identified proteins increased significantly when the IEF fractionation step was included as part of the platform. Relevant proteins with biological and disease significance were observed and the dynamic range of the serum proteome measurement was extended. In addition, potential glycan changes were indicated by comparing proteins in control and cancer samples in terms of their affinity to the multi-lectin column (M-LAC) and the pI profiles in IEF separation. In conclusion, a proteomics platform including high abundance protein depletion, lectin affinity fractionation, IEF separation, and LC-MS analysis has been applied to discover breast cancer-associated proteins. The following candidates, thrombospondin-1 and 5, alpha-1B-glycoprotein, serum amyloid P-component, and tenascin-X, were selected as promising examples of the use of this platform. They show potential abundance and glycan changes and will be further investigated in future studies.

Indexed as

Biomarkers, TumorBreast NeoplasmsCartilage Oligomeric Matrix ProteinChromatography, AffinityChromatography, High Pressure LiquidExtracellular Matrix ProteinsFemaleGlycoproteinsHumansIsoelectric FocusingLectinsMass SpectrometryMatrilin ProteinsProteomeSerum Amyloid P-ComponentTenascinBiomarkers, TumorCartilage Oligomeric Matrix ProteinExtracellular Matrix ProteinsGlycoproteinsLectinsMatrilin ProteinsProteomeSerum Amyloid P-ComponentTenascintenascin XThrombospondin 1TSP5 protein, human

Identifiers

PMID21513341
PMCPMC3148019
OpenAlexW2019476683

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Registered trials

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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.