Evidence map›Paper›PMID 23223448›Full record

ArticleThe Journal of biological chemistry2013

Loss of LARGE2 disrupts functional glycosylation of α-dystroglycan in prostate cancer.

Alison K Esser, Michael R Miller, Qin Huang, Melissa M Meier, Daniel Beltran-Valero de Bernabé, Christopher S Stipp, Kevin P Campbell, Charles F Lynch, Brian J Smith, Michael B Cohen and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

32 citing papers in PubMed, 44 citations in OpenAlex.

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  20. CDP-glycerol inhibits the synthesis of the functionalThe Journal of biological chemistry · 2018
    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

11 authors at 1 institution in 2 countries.

Alison K EsserDepartment of Molecular Physiology and Biophysics, The Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242, USA.
Michael R Miller
Qin Huang
Melissa M Meier
Daniel Beltran-Valero de Bernabé
Christopher S Stipp
Kevin P Campbell
Charles F Lynch
Brian J Smith
Michael B Cohen
Michael D Henry
University of Iowa · US

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Douglas Robert Spitz · 2000 to 2026
$70.0M
TRANSCRIPTOME AND PROTEOME STRATIFICATION OF PROSTATE ADENOCARCINOMA PHENOTYPESP50CA097186 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI John Kyung Lee · 2002 to 2026
$58.1M
Pulmonary Toxicology Facility CoreP30ES005605 · NIEHS · UNIVERSITY OF IOWA · PI Brandi Janssen · 1990 to 2026
$40.5M
MOLECULAR ONCOLOGY TRAINING GRANTT32CA113275 · NCI · WASHINGTON UNIVERSITY · PI Matthew J Walter · 2006 to 2026
$5.7M
Predoctoral Training in the Pharmacological SciencesT32GM067795 · NIGMS · UNIVERSITY OF IOWA · PI STRACK, STEFAN · 2004 to 2021
$3.4M
Role of Dystroglycan in Prostate Cancer ProgressionR01CA130916 · NCI · UNIVERSITY OF IOWA · PI HENRY, MICHAEL D · 2008 to 2012
$1.6M
Dissecting the opposing roles of alpha-3 integrin in metastasisR01CA136664 · NCI · UNIVERSITY OF IOWA · PI STIPP, CHRISTOPHER S. · 2009 to 2013
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS CA097186NCI NIH HHS HHSN261201000032CNCI NIH HHS P30 CA086862NCI NIH HHS P50 CA097186NCI NIH HHS R01 CA130916NCI NIH HHS R01CA130916NCI NIH HHS R01 CA136664NCI NIH HHS T32 CA113275NIEHS NIH HHS P30 ES005605NIGMS NIH HHS T32 GM067795
6 · The paper itself

Abstract

Dystroglycan (DG) is a cell surface receptor for extracellular matrix proteins and is involved in cell polarity, matrix organization, and mechanical stability of tissues. Previous studies documented loss of DG protein expression and glycosylation in a variety of cancer types, but the underlying mechanisms and the functional consequences with respect to cancer progression remain unclear. Here, we show that the level of expression of the βDG subunit as well as the glycosylation status of the αDG subunit inversely correlate with the Gleason scores of prostate cancers; furthermore, we show that the functional glycosylation of αDG is substantially reduced in prostate cancer metastases. Additionally, we demonstrate that LARGE2 (GYLTL1B), a gene not previously implicated in cancer, regulates functional αDG glycosylation in prostate cancer cell lines; knockdown of LARGE2 resulted in hypoglycosylation of αDG and loss of its ability to bind laminin-111 while overexpression restored ligand binding and diminished growth and migration of an aggressive prostate cancer cell line. Finally, our analysis of LARGE2 expression in human cancer specimens reveals that LARGE2 is significantly down-regulated in the context of prostate cancer, and that its reduction correlates with disease progression. Our results describe a novel molecular mechanism to account for the commonly observed hypoglycosylation of αDG in prostate cancer.

Indexed as

Gene Expression Regulation, NeoplasticCell Line, TumorCell MovementCell ProliferationCell SeparationDisease ProgressionDystroglycansEpitheliumExtracellular MatrixFlow CytometryGlycosylationGlycosyltransferasesHumansImmunohistochemistryLamininMaleDystroglycansGlycosyltransferasesLamininLARGE2 protein, humanMembrane ProteinsRNA, Small Interfering

Identifiers

PMID23223448
PMCPMC3554886
OpenAlexW2159631682

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.