Evidence map›Paper›PMID 23775902›Full record

ArticleProteomics. Clinical applications2013

Increased bisecting N-acetylglucosamine and decreased branched chain glycans of N-linked glycoproteins in expressed prostatic secretions associated with prostate cancer progression.

Julius O Nyalwidhe, Lucy R Betesh, Thomas W Powers, E Ellen Jones, Krista Y White, Tanya C Burch, Jasmin Brooks, Megan T Watson, Raymond S Lance, Dean A Troyer and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed, 80 citations in OpenAlex.

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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

13 authors at 3 institutions in 1 country.

Julius O NyalwidheDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA , USA.
Lucy R BeteshDepartment of Microbiology and Immunology, Drexel Institute for Biotechnology and Virology, Drexel University College of Medicine, Doylestown, PA, USA.
Thomas W PowersDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, MUSC Proteomics Center, Medical University of South Carolina, Charleston, SC, USA.
E Ellen JonesDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, MUSC Proteomics Center, Medical University of South Carolina, Charleston, SC, USA.
Krista Y WhiteDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA.
Tanya C BurchDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA.
Jasmin BrooksDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, MUSC Proteomics Center, Medical University of South Carolina, Charleston, SC, USA.
Megan T WatsonDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA.
Raymond S LanceThe Leroy T. Canoles, Jr. Cancer Research Center, Eastern Virginia Medical School Norfolk, VA, USA.
Dean A TroyerThe Leroy T. Canoles, Jr. Cancer Research Center, Eastern Virginia Medical School Norfolk, VA, USA.
O John SemmesDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA.
Anand MehtaDepartment of Microbiology and Immunology, Drexel Institute for Biotechnology and Virology, Drexel University College of Medicine, Doylestown, PA, USA.
Richard R DrakeDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, MUSC Proteomics Center, Medical University of South Carolina, Charleston, SC, USA.
Eastern Virginia Medical School · USMedical University of South Carolina · USDrexel University · US

Funding

Translational Science Laboratory Shared ResourceP30CA138313 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI RAYMOND N. DUBOIS · 2009 to 2026
$42.7M
Predicting HCC through GlycomicsR01CA120206 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2006 to 2016
$4.3M
Aberrantly secreted glycoproteins as markers of liver cancerU01CA168856 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2012 to 2016
$1.5M
Glycan Biomarkers of Prostate Cancer in Prostatic FluidsR01CA135087 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DRAKE, RICHARD R. · 2009 to 2012
$989k
Proximal Prostate Fluids for Protein and miRNA BiomarkersR21CA137704 · NCI · EASTERN VIRGINIA MEDICAL SCHOOL · PI DRAKE, RICHARD R. · 2009 to 2010
$347k
NCI NIH HHS P30 CA138313NCI NIH HHS R01 CA120206NCI NIH HHS R01 CA135087NCI NIH HHS R01CA135087NCI NIH HHS R21 CA137704NCI NIH HHS R21CA137704NCI NIH HHS U01 CA168856
6 · The paper itself

Abstract

purposeUsing prostatic fluids rich in glycoproteins like prostate-specific antigen and prostatic acid phosphatase (PAP), the goal of this study was to identify the structural types and relative abundance of glycans associated with prostate cancer status for subsequent use in emerging MS-based glycopeptide analysis platforms. EXPERIMENTAL

designA series of pooled samples of expressed prostatic secretions (EPS) and exosomes reflecting different stages of prostate cancer disease were used for N-linked glycan profiling by three complementary methods, MALDI-TOF profiling, normal-phase HPLC separation, and triple quadropole MS analysis of PAP glycopeptides.

resultsGlycan profiling of N-linked glycans from different EPS fluids indicated a global decrease in larger branched tri- and tetra-antennary glycans. Differential exoglycosidase treatments indicated a substantial increase in bisecting N-acetylglucosamines correlated with disease severity. A triple quadrupole MS analysis of the N-linked glycopeptides sites from PAP in aggressive prostate cancer pools was done to cross-reference with the glycan profiling data. CONCLUSION AND CLINICAL RELEVANCE: Changes in glycosylation as detected in EPS fluids reflect the clinical status of prostate cancer. Defining these molecular signatures at the glycopeptide level in individual samples could improve current approaches of diagnosis and prognosis.

Indexed as

Disease ProgressionAcetylglucosamineGlycomicsGlycoproteinsHumansMaleNeoplasm GradingPolysaccharidesProstateProstatic NeoplasmsAcetylglucosamineGlycoproteinsPolysaccharidesExpressed prostatic secretionGlycomicsN-linked glycosylationProstate cancerUrine exosome

Identifiers

PMID23775902
PMCPMC3969874
OpenAlexW2094056333

What OpenQuestion holds

Textmetadata
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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.