Evidence map›Paper›PMID 28601093›Full record

ArticleBMC cancer2017

Granulin-epithelin precursor interacts with 78-kDa glucose-regulated protein in hepatocellular carcinoma.

Chi Wai Yip, Ching Yan Lam, Terence C W Poon, Tan To Cheung, Phyllis F Y Cheung, Sze Wai Fung, Xiao Qi Wang, Idy C Y Leung, Linda W C Ng, Chung Mau Lo and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC cancer, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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

12 authors at 4 institutions in 3 countries.

Chi Wai YipDepartment of Surgery, The Chinese University of Hong Kong, Hong Kong, China.
Ching Yan LamDepartment of Surgery, The University of Hong Kong, Hong Kong, China.
Terence C W PoonFaculty of Health Sciences, University of Macau, Macau, China.
Tan To CheungDepartment of Surgery, The University of Hong Kong, Hong Kong, China.
Phyllis F Y CheungDepartment of Surgery, The Chinese University of Hong Kong, Hong Kong, China.
Sze Wai FungDepartment of Surgery, The Chinese University of Hong Kong, Hong Kong, China.
Xiao Qi WangDepartment of Surgery, The University of Hong Kong, Hong Kong, China.
Idy C Y LeungDepartment of Surgery, The University of Hong Kong, Hong Kong, China.
Linda W C NgDepartment of Surgery, The Chinese University of Hong Kong, Hong Kong, China.
Chung Mau LoDepartment of Surgery, The University of Hong Kong, Hong Kong, China.
George S W TsaoSchool of Biomedical Sciences, The University of Hong Kong, Hong Kong, China.
Siu Tim CheungDepartment of Surgery, The Chinese University of Hong Kong, Hong Kong, China. stcheung@surgery.cuhk.edu.hk.
University of Hong Kong · HKChinese University of Hong Kong · CNDepartment of Health · CNUniversity of Macau · MO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGranulin-epithelin precursor (GEP) is a secretory growth factor, which has been demonstrated to control cancer growth, invasion, drug resistance and immune escape. Our previous studies and others also demonstrated its potential in targeted therapy. Comprehensive characterization of GEP partner on cancer cells are warranted. We have previously shown that GEP interacted with heparan sulfate on the surface of liver cancer cells and the interaction is crucial for GEP-mediated signaling transduction. This study aims to characterize GEP protein partner at the cell membrane with the co-immunoprecipitation and mass spectrometry approach.

methodsThe membrane fraction from liver cancer model Hep3B was used for capturing binding partner with the specific monoclonal antibody against GEP. The precipitated proteins were analyzed by mass spectrometry. After identifying the GEP binding partner, this specific interaction was validated in additional liver cancer cell line HepG2 by co-immunoprecipitation using GRP78 and GEP antibodies, respectively, as the bait. GRP78 transcript levels in hepatocellular carcinoma (HCC) clinical samples (n = 77 pairs) were examined by real-time quantitative RT-PCR. GEP and GRP78 protein expressions were investigated by immunohistochemistry on paraffin sections.

resultsWe identified the GEP-binding protein as 78-kDa glucose-regulated protein (GRP78, also named heat shock 70-kDa protein 5, HSPA5). This interaction was validated in independent HCC cell lines. Increased GRP78 mRNA levels were demonstrated in liver cancer tissues compared with the paralleled liver tissues (t-test, P = 0.002). GRP78 and GEP transcript levels were significantly correlated (Spearman's correlation, P = 0.001), and the proteins were also detectable in the cytoplasm of liver cancer cells by immunohistochemical staining.

conclusionsGRP78 and GEP are interacting protein partners in liver cancer cells and may play a role in GEP-mediated cancer progression in HCC.

Indexed as

Signal TransductionCarcinoma, HepatocellularCell Line, TumorEndoplasmic Reticulum Chaperone BiPFemaleGene Expression Regulation, NeoplasticHeat-Shock ProteinsHep G2 CellsHumansIntercellular Signaling Peptides and ProteinsLiver NeoplasmsMaleMiddle AgedProgranulinsProtein BindingEndoplasmic Reticulum Chaperone BiPGRN protein, humanHeat-Shock ProteinsHSPA5 protein, humanIntercellular Signaling Peptides and ProteinsProgranulins78-kDa glucose-regulated proteinGranulin-epithelin precursorHepatocellular carcinomaMass spectrometryProtein interaction

Identifiers

PMID28601093
PMCPMC5466756
OpenAlexW2623277518

What OpenQuestion holds

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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.