Evidence map›Paper›PMID 24854630›Full record

ArticleThe Prostate2014

Increased expression of GCNT1 is associated with altered O-glycosylation of PSA, PAP, and MUC1 in human prostate cancers.

Zuxiong Chen, Zulfiqar G Gulzar, Catherine A St Hill, Bruce Walcheck, James D Brooks

Open access · greenAbstract read
In one paragraph

Article in The Prostate, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
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  11. Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023
    Review
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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

5 authors at 2 institutions in 1 country.

Zuxiong ChenDepartment of Urology, Stanford University, Stanford, California.
Zulfiqar G Gulzar
Catherine A St Hill
Bruce Walcheck
James D Brooks
Stanford University · USUniversity of Minnesota · US

Funding

New Tools for Prostate Cancer Detection and PrognosticationU01CA152737 · NCI · STANFORD UNIVERSITY · PI BROOKS, JAMES D., GAMBHIR, SANJIV S · 2010 to 2015
$2.8M
Regulation of inflammation: sheddases and CD62LR01HL061613 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WALCHECK, BRUCE K · 2000 to 2009
$2.5M
NCI NIH HHS 1U01CA152737-01NCI NIH HHS U01 CA152737NHLBI NIH HHS R01 HL061613
6 · The paper itself

Abstract

backgroundProtein glycosylation is a common posttranslational modification and glycan structural changes have been observed in several malignancies including prostate cancer. We hypothesized that altered glycosylation could be related to differences in gene expression levels of glycoprotein synthetic enzymes between normal and malignant prostate tissues.

methodsWe interrogated prostate cancer gene expression data for reproducible changes in expression of glycoprotein synthetic enzymes. Over-expression of GCNT1 was validated in prostate samples using RT-PCR. ELISA was used to measure core 2 O-linked glycan sialyl Lewis X (sLe(x) ) of prostate specific antigen (PSA), Mucin1 (MUC1), and prostatic acidic phosphatase (PAP) proteins.

resultsA key glycosyltransferase, GCNT1, was consistently over-expressed in several prostate cancer gene expression datasets. RT-PCR confirmed increased transcript levels in cancer samples compared to normal prostate tissue in fresh-frozen prostate tissue samples. ELISA using PSA, PAP, and MUC1 capture antibodies and a specific core 2 O-linked sLe(x) detection antibody demonstrated elevation of this glycan structure in cancer compared to normal tissues for MUC1 (P = 0.01), PSA (P = 0.03) and near significant differences in PAP sLe(x) levels (P = 0.06). MUC1, PSA and PAP protein levels alone were not significantly different between paired normal and malignant prostate samples.

conclusionsGCNT1 is over-expressed in prostate cancer and is associated with higher levels of core 2 O-sLe(x) in PSA, PAP and MUC1 proteins. Alterations of O-linked glycosylation could be important in prostate cancer biology and could provide a new avenue for development of prostate cancer specific glycoprotein biomarkers.

Indexed as

Acid PhosphataseAgedGlycosylationHumansLewis X AntigenMaleMiddle AgedMucin-1N-AcetylglucosaminyltransferasesProstate-Specific AntigenProstatic NeoplasmsProtein Tyrosine PhosphatasesSialyl Lewis X AntigenAcid Phosphatasebeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-acetylglucosaminyl transferaseLewis X AntigenMUC1 protein, humanMucin-1N-AcetylglucosaminyltransferasesProstate-Specific Antigenprostatic acid phosphataseProtein Tyrosine PhosphatasesSialyl Lewis X AntigenGCNT1O-glycosylationprostate cancersialyl Lewis X

Identifiers

PMID24854630
PMCPMC5862140
OpenAlexW1885032802

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.