Evidence map›Paper›PMID 19377061›Full record

ArticleMolecular & cellular proteomics : MCP2009

The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays.

Tingting Yue, Irwin J Goldstein, Michael A Hollingsworth, Karen Kaul, Randall E Brand, Brian B Haab

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

79 citing papers in PubMed, 134 citations in OpenAlex.

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  13. Current State of "Omics" Biomarkers in Pancreatic Cancer.Journal of personalized medicine · 2021
    Review
  14. Article
  15. High Expression of N-Acetylgalactosaminyl-transferase 1 (GALNT1) Associated with Invasion, Metastasis, and Proliferation in Osteosarcoma.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article
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19 more citing papers are in PubMed but not listed here.

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

6 authors at 6 institutions in 1 country.

Tingting YueVan Andel Research Institute, Grand Rapids, Michigan 49503, USA.
Irwin J Goldstein
Michael A Hollingsworth
Karen Kaul
Randall E Brand
Brian B Haab
Michigan State University · USNorthShore University HealthSystem · USUniversity of Michigan–Ann Arbor · USUniversity of Nebraska Medical Center · USUniversity of Pittsburgh Medical Center · USVan Andel Institute · US

Funding

PROTEIN/CARBOHYDRATE INTERACTIONR01GM029470 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GOLDSTEIN, IRWIN J · 1985 to 2007
$2.4M
Defining Secreted Glycan Alterations in Pancreatic CancerR33CA122890 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI HAAB, BRIAN B. · 2008 to 2010
$894k
Defining Secreted Glycan Alterations in Pancreatic CancerR21CA122890 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI HAAB, BRIAN B. · 2006 to 2006
$325k
NCI NIH HHS R21 CA122890NCI NIH HHS R33 CA122890NIGMS NIH HHS GM 29470NIGMS NIH HHS R01 GM029470
6 · The paper itself

Abstract

Changes to the glycan structures of proteins secreted by cancer cells are known to be functionally important and to have potential diagnostic value. However, an exploration of the population variation and prevalence of glycan alterations on specific proteins has been lacking because of limitations in conventional glycobiology methods. Here we report the use of a previously developed antibody-lectin sandwich array method to characterize both the protein and glycan levels of specific mucins and carcinoembryonic antigen-related proteins captured from the sera of pancreatic cancer patients (n = 23) and control subjects (n = 23). The MUC16 protein was frequently elevated in the cancer patients (65% of the patients) but showed no glycan alterations, whereas the MUC1 and MUC5AC proteins were less frequently elevated (30 and 35%, respectively) and showed highly prevalent (up to 65%) and distinct glycan alterations. The most frequent glycan elevations involved the Thomsen-Friedenreich antigen, fucose, and Lewis antigens. An unexpected increase in the exposure of alpha-linked mannose also was observed on MUC1 and MUC5ac, indicating possible N-glycan modifications. Because glycan alterations occurred independently from the protein levels, improved identification of the cancer samples was achieved using glycan measurements on specific proteins relative to using the core protein measurements. The most significant elevation was the cancer antigen 19-9 on MUC1, occurring in 19 of 23 (87%) of the cancer patients and one of 23 (4%) of the control subjects. This work gives insight into the prevalence and protein carriers of glycan alterations in pancreatic cancer and points to the potential of using glycan measurements on specific proteins for highly effective biomarkers.

Indexed as

AntibodiesAntigens, NeoplasmArea Under CurveBiomarkers, TumorCarbohydrate ConformationGene Expression ProfilingGlycoproteinsHumansImmunoassayLectinsMicroarray AnalysisMucin 5ACPancreatic NeoplasmsPolysaccharidesProtein BindingAntibodiesAntigens, NeoplasmBiomarkers, TumorGlycoproteinsLectinsMUC5AC protein, humanMucin 5ACPolysaccharides

Identifiers

PMID19377061
PMCPMC2709194
OpenAlexW2164572761

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.