Evidence map›Paper›PMID 28701735›Full record

ArticleScientific reports2017

Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma.

Mingchao Wang, Fang Tian, Wantao Ying, Xiaohong Qian

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
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  10. Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
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  16. The functional role of exosome in hepatocellular carcinoma.Journal of cancer research and clinical oncology · 2018
    Review
  17. 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

4 authors at 1 institution in 1 country.

Mingchao WangBeijing Institute of Radiation Medicine, National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China.
Fang TianBeijing Institute of Radiation Medicine, National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China.
Wantao YingBeijing Institute of Radiation Medicine, National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China. proteomics@126.com.
Xiaohong QianBeijing Institute of Radiation Medicine, National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China. qianxh1@163.com.YING.
Beijing Proteome Research Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatocellular carcinoma (HCC) is a serious threat to human health. The carbohydrate recognition domain of Galectin-3 (Gal3C) has been reported to be an anti-tumour molecule. In this study, we aim to explore effects of Gal3C in HCC and its possible molecular mechanism with quantitative proteomics approach. We found that rGal3C stimulation could inhibit cell viability, migration and invasion of HepG2. After rGal3C stimulating, 190 proteins were differentially expressed. Eighty up-regulated proteins located mainly in extracellular exosome and involved in cell adhesion and metabolism, and 110 down-regulated proteins located in mitochondria and extracellular exosome, and related to processes of metabolism and oxidation-reduction. Of the differentially expressed proteins, CLU, NDRG1, CD166, S100A11 and Galectin-1 were carcinoma-related proteins affected by rGal3C. Potential receptors of rGal3C were explored by an UV cross-linking capture strategy. We showed that rGal3C could induce dephosphorylating of FAK/SRC. Blocking of the FAK/SRC pathway resulted in down-regulation of NDRG1. Immunofluorescence suggested that rGal3C could disrupt integrin clustering. Our study provides valuable insight into the anti-tumour mechanism of rGal3C in HCC on a proteomics level and is the first to reveal the possible mechanism involving integrin/FAK/SRC pathway and NDRG1. These results provide useful guidance of developing new therapies for HCC.

Indexed as

Carbohydrate MetabolismProtein Interaction Domains and MotifsProteomeProteomicsBlood ProteinsCarcinoma, HepatocellularCell Line, TumorCell MovementCell ProliferationComputational BiologyData MiningFocal Adhesion Kinase 1Galectin 3GalectinsHep G2 CellsHumansBlood ProteinsFocal Adhesion Kinase 1Galectin 3GalectinsLGALS3 protein, humanProteomePTK2 protein, humansrc-Family Kinases

Identifiers

PMID28701735
PMCPMC5507876
OpenAlexW2734079315

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Registered trials

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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.