Evidence map›Paper›PMID 26336134›Full record

ArticleOncotarget2015

Histidine-rich glycoprotein function in hepatocellular carcinoma depends on its N-glycosylation status, and it regulates cell proliferation by inhibiting Erk1/2 phosphorylation.

Qinle Zhang, Kai Jiang, Yan Li, Dongmei Gao, Lu Sun, Shu Zhang, Tianhua Liu, Kun Guo, Yinkun Liu

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. GALNT6 suppresses progression of colorectal cancer.American journal of cancer research · 2018
    Article
  14. 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

9 authors at 5 institutions in 1 country.

Qinle ZhangLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Kai JiangLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Yan LiLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Dongmei GaoLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Lu SunCancer Research Center, Institute of Biomedical Science, Fudan University, Shanghai 200032, China.
Shu ZhangLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Tianhua LiuLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Kun GuoLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Yinkun LiuLiver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
Fudan University Shanghai Cancer Center · CNSun Yat-sen University · CNThe First Affiliated Hospital, Sun Yat-sen University · CNZhongshan Hospital · CNFudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatocellular carcinoma (HCC) is the third most common cause of cancer mortality. Significantly downregulated histidine-rich glycoprotein (HRG) during the dynamic stages (WB, WB7, and WB11) of neoplastic transformation of WB F344 hepatic oval-like cells was screened out by iTRAQ labeling followed by 2DLC-ESI-MS/MS analysis. HRG expression was significantly lower in HCC tissues. HRG overexpression in Huh7 and MHCC-97H hepatoma cell lines led to decreased cell proliferation, colony-forming ability, and tumor growth, and increased cell apoptosis. HRG could inhibit cell proliferation via the FGF-Erk1/2 signaling pathway by reducing Erk1/2 phosphorylation. On the other hand, the functional expression of HRG was also dependent on the glycosylation status at its N-terminal, especially at the glycosylation site Asn 125. The glycosylation of HRG may play a key competitive role in the interaction between HRG and heparin sulfate for binding bFGF and activating the FGF receptor. These findings provide novel insights into the molecular mechanism of HRG in HCC.

Indexed as

Cell ProliferationProtein Processing, Post-TranslationalAnimalsApoptosisCarcinoma, HepatocellularCell Line, TumorGlycosylationHistidine-Rich GlycoproteinHumansLiver NeoplasmsMice, NudeMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PhosphorylationProteinsProteomicsHistidine-Rich GlycoproteinMAPK1 protein, humanMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Proteinscell proliferationglycosylationhepatocellular carcinomahistidine-rich glycoprotein

Identifiers

PMID26336134
PMCPMC4745792
OpenAlexW1937612777

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.