Evidence map›Paper›PMID 30110170›Full record

ArticleJournal of proteome research2018

N-Linked Glycan Branching and Fucosylation Are Increased Directly in Hcc Tissue As Determined through in Situ Glycan Imaging.

Connor A West, Mengjun Wang, Harmin Herrera, Hongyan Liang, Alyson Black, Peggi M Angel, Richard R Drake, Anand S Mehta

Abstract read
In one paragraph

Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 73 citations in OpenAlex.

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  13. Prospective on Imaging Mass Spectrometry in Clinical Diagnostics.Molecular & cellular proteomics : MCP · 2023
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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

8 authors at 2 institutions in 1 country.

Connor A WestMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.
Mengjun WangMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.
Harmin HerreraGraduate School of Biomedical Sciences and Professional Studies, Drexel University College of Medicine , Department of Microbiology and Immunology , 2900 Queen Lane , Philadelphia , Pennsylvania 19129 , United States.
Hongyan LiangMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.
Alyson BlackMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.
Peggi M AngelMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.ORCID 0000-0002-4436-555X
Richard R DrakeMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.
Anand S MehtaMedical University of South Carolina , Department of Cell and Molecular Pharmacology , 173 Ashley Avenue BSB 358 , Charleston , South Carolina 29425 , United States.ORCID 0000-0002-9846-9389
Medical University of South Carolina · USDrexel University · US

Funding

Predicting HCC through GlycomicsR01CA120206 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2006 to 2016
$4.3M
Glycopathology of HCC: identification of the source cells of serum fucosylationU01CA226052 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DRAKE, RICHARD R., HOSHIDA, YUJIN · 2019 to 2023
$2.8M
Aberrantly secreted glycoproteins as markers of liver cancerU01CA168856 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2012 to 2016
$1.5M
NCI NIH HHS F31 CA250266NCI NIH HHS R01 CA120206NCI NIH HHS U01 CA168856NCI NIH HHS U01 CA226052
6 · The paper itself

Abstract

Hepatocellular carcinoma (HCC) remains as the fifth most common cancer in the world and accounts for more than 700,000 deaths annually. Changes in serum glycosylation have long been associated with this cancer but the source of that material is unknown and direct glycan analysis of HCC tissues has been limited. Our laboratory previously developed a method of in situ tissue based N-linked glycan imaging that bypasses the need for microdissection and solubilization of tissue prior to analysis. We used this methodology in the analysis of 138 HCC tissue samples and compared the N-linked glycans in cancer tissue with either adjacent untransformed or tissue from patients with liver cirrhosis but no cancer. Ten glycans were found significantly elevated in HCC tissues as compared to cirrhotic or adjacent tissue. These glycans fell into two major classes, those with increased levels of fucosylation and those with increased levels of branching with or without any fucose modifications. In addition, increased levels of fucosylated glycoforms were associated with a reduction in survival time. This work supports the hypothesis that the increased levels of fucosylated N-linked glycans in HCC serum are produced directly from the cancer tissue.

Indexed as

AdultCarcinoma, HepatocellularFemaleFucoseGlycosylationHistocytochemistryHumansKaplan-Meier EstimateLiverLiver CirrhosisLiver NeoplasmsMaleMiddle AgedPolysaccharidesTissue Array AnalysisFucosePolysaccharidesglycanMALDItumor

Identifiers

PMID30110170
PMCPMC6784322
OpenAlexW2886344763

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.