Evidence map›Paper›PMID 28665748›Full record

ArticleCancer biology & therapy2017

SUMOylation of HSP27 by small ubiquitin-like modifier 2/3 promotes proliferation and invasion of hepatocellular carcinoma cells.

Haize Ge, Juan Du, Jingman Xu, Xiangliang Meng, Jinchuan Tian, Jie Yang, Huimin Liang

Open access · bronzeAbstract read
In one paragraph

Article in Cancer biology & therapy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Abnormal protein SUMOylation in liver disease: novel target for therapy.Journal of molecular medicine (Berlin, Germany) · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
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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

7 authors at 3 institutions in 1 country.

Haize Gea Department of Clinical Laboratory, the Third Central Hospital of Tianjin.
Juan Dub Tianjin Key Laboratory of Artificial Cell.
Jingman Xuf Heart Institute, Medical Experimental Research Center , North China University of Science and Technology , Tangshan , Hebei , China.
Xiangliang Menga Department of Clinical Laboratory, the Third Central Hospital of Tianjin.
Jinchuan Tiana Department of Clinical Laboratory, the Third Central Hospital of Tianjin.
Jie Yanga Department of Clinical Laboratory, the Third Central Hospital of Tianjin.
Huimin Liangd School of Nursing , Tianjin Medical University , Tianjin , China.
Tianjin Medical University · CNTianjin Third Central Hospital · CNNorth China University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Primary hepatocellular carcinoma (PHC) is a major health problem worldwide and is one of the 10 most commonly diagnosed cancers in China. Heat shock protein 27 (HSP27) were found to be overexpressed in a wide range of malignancies including PHC, however, post-translational modification of HSP27 still needs exploration in PHC. Recently, SUMOylation, an important post-translational modification associating with the development of many kinds of cancers has been intensively studied. In the current study, mRNA and protein level of HSP27 in archived tumor samples representing various pathological characteristics of PHC were examined, and modification of HSP27 by SUMO2/3 was investigated. HSP27 were expressed abundantly in patients' tumor tissues, and found to be associated with pathological progression. Besides, HSP27 was also elevated significantly in liver cancer cell lines Huh7 and HepG2 compared with human hepatocyte cells L02. Furthermore, knockdown of HSP27 was found to be associated with the decreased proliferation and invasion ability in Huh7 and HepG2 cells. Immunofluorescence assay showed that HSP27 and SUMO2/3 were co-localized in the subcellular, and co-immunoprecipitation verified the interaction between HSP27 and SUMO2/3. Overexpression of SUMO2/3 upregulated the HSP27 protein level and promotes Huh7 and HepG2 cell proliferation and invasion, and vice versa when the SUMO2/3 was knockdown. Taken together, increased protein level of HSP27 through SUMO2/3-mediated SUMOylation plays crucial roles in the progression of PHC, and this finding may shed light on developing potential therapeutic targets for PHC.

Indexed as

Carcinoma, HepatocellularCell ProliferationChinaDisease ProgressionFemaleGene Knockdown TechniquesHeat-Shock ProteinsHepatocytesHep G2 CellsHSP27 Heat-Shock ProteinsHumansImmunoprecipitationIncidenceLiver NeoplasmsMaleMiddle AgedHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanMolecular ChaperonesRNA, MessengerSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanUbiquitinsHSP27liver cancerSUMO2/3SUMOylation

Identifiers

PMID28665748
PMCPMC5653183
OpenAlexW2728414219

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.