Evidence map›Paper›PMID 27046040›Full record

ArticlePloS one2016

Phosphorylated Heat Shock Protein 20 (HSPB6) Regulates Transforming Growth Factor-α-Induced Migration and Invasion of Hepatocellular Carcinoma Cells.

Rie Matsushima-Nishiwaki, Hidenori Toyoda, Tomoaki Nagasawa, Eisuke Yasuda, Naokazu Chiba, Seiji Okuda, Atsuyuki Maeda, Yuji Kaneoka, Takashi Kumada, Osamu Kozawa

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

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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

10 authors at 3 institutions in 1 country.

Rie Matsushima-NishiwakiDepartment of Pharmacology, Gifu University Graduate School of Medicine, Gifu, Japan.
Hidenori ToyodaDepartment of Gastroenterology, Ogaki Municipal Hospital, Ogaki, Gifu, Japan.
Tomoaki NagasawaDepartment of Pharmacology, Gifu University Graduate School of Medicine, Gifu, Japan.
Eisuke YasudaDepartment of Radiological Technology, Suzuka University of Medical Science, Suzuka, Mie, Japan.
Naokazu ChibaDepartment of Pharmacology, Gifu University Graduate School of Medicine, Gifu, Japan.
Seiji OkudaDepartment of Medical Technology, Ogaki Municipal Hospital, Ogaki, Gifu, Japan.
Atsuyuki MaedaDepartment of Surgery, Ogaki Municipal Hospital, Ogaki, Gifu, Japan.
Yuji KaneokaDepartment of Surgery, Ogaki Municipal Hospital, Ogaki, Gifu, Japan.
Takashi KumadaDepartment of Gastroenterology, Ogaki Municipal Hospital, Ogaki, Gifu, Japan.
Osamu KozawaDepartment of Pharmacology, Gifu University Graduate School of Medicine, Gifu, Japan.
Ogaki Municipal Hospital · JPGifu University · JPSuzuka University of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human hepatocellular carcinoma (HCC) is one of the major malignancies in the world. Small heat shock proteins (HSPs) are reported to play an important role in the regulation of a variety of cancer cell functions, and the functions of small HSPs are regulated by post-translational modifications such as phosphorylation. We previously reported that protein levels of a small HSP, HSP20 (HSPB6), decrease in vascular invasion positive HCC compared with those in the negative vascular invasion. Therefore, in the present study, we investigated whether HSP20 is implicated in HCC cell migration and the invasion using human HCC-derived HuH7 cells. The transforming growth factor (TGF)-α-induced migration and invasion were suppressed in the wild-type-HSP20 overexpressed cells in which phosphorylated HSP20 was detected. Phospho-mimic-HSP20 overexpression reduced the migration and invasion compared with unphosphorylated HSP20 overexpression. Dibutyryl cAMP, which enhanced the phosphorylation of wild-type-HSP20, significantly reduced the TGF-α-induced cell migration of wild-type HSP20 overexpressed cells. The TGF-α-induced cell migration was inhibited by SP600125, a c-Jun N-terminal kinases (JNK) inhibitor. In phospho-mimic-HSP20 overexpressed HuH7 cells, TGF-α-stimulated JNK phosphorylation was suppressed compared with the unphosphorylated HSP20 overexpressed cells. Moreover, the level of phospho-HSP20 protein in human HCC tissues was significantly correlated with tumor invasion. Taken together, our findings strongly suggest that phosphorylated HSP20 inhibits TGF-α-induced HCC cell migration and invasion via suppression of the JNK signaling pathway.

Indexed as

Cell MovementAnthracenesCarcinoma, HepatocellularCell Line, TumorGene Expression Regulation, NeoplasticHSP27 Heat-Shock ProteinsHumansLiver NeoplasmsMAP Kinase Kinase 4Neoplasm InvasivenessNeoplasm ProteinsPhosphorylationSignal TransductionTransforming Growth Factor alphaAnthracenesHSP27 Heat-Shock ProteinsHSPB7 protein, humanMAP Kinase Kinase 4Neoplasm ProteinspyrazolanthroneTransforming Growth Factor alpha

Identifiers

PMID27046040
PMCPMC4821579
OpenAlexW2321456449

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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.