Evidence map›Paper›PMID 26859835›Full record

ArticlePloS one2016

Heat Shock Protein 27 Plays a Pivotal Role in Myofibroblast Differentiation and in the Development of Bleomycin-Induced Pulmonary Fibrosis.

Ah-Mee Park, Kyosuke Kanai, Tatsuki Itoh, Takao Sato, Tatsuya Tsukui, Yutaka Inagaki, Moises Selman, Kouji Matsushima, Osamu Yoshie

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.1field-weighted citation impact, top 6% 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, 39 citations in OpenAlex.

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  11. Mesenchymal MAPKAPK2/HSP27 drives intestinal carcinogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

9 authors at 4 institutions in 2 countries.

Ah-Mee ParkDepartment of Microbiology and Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan.
Kyosuke KanaiDepartment of Microbiology and Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan.
Tatsuki ItohDepartment of Pathology, Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan.
Takao SatoDepartment of Pathology, Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan.
Tatsuya TsukuiDepartment of Molecular Preventive Medicine, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.
Yutaka InagakiDepartment of Regenerative Medicine, Tokai University School of Medicine, Sagamihara, Kanagawa, Japan.
Moises SelmanInstituto Nacional de Enfermedades Respiratorias, México DF, Mexico.
Kouji MatsushimaDepartment of Molecular Preventive Medicine, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.
Osamu YoshieDepartment of Microbiology and Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan.
Kindai University · JPThe University of Tokyo · JPInstituto Nacional de Enfermedades Respiratorias · MXTokai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-β1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with α-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and α-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases.

Indexed as

ActinsAgedAnimalsBleomycinCell DifferentiationCell LineCollagen Type IFemaleFibroblastsFibronectinsGene Knockdown TechniquesHSP27 Heat-Shock ProteinsHumansIdiopathic Pulmonary FibrosisMaleMiceACTA2 protein, humanActinsBleomycinCollagen Type IFibronectinsHSP27 Heat-Shock ProteinsOsteopontinTransforming Growth Factor beta1

Identifiers

PMID26859835
PMCPMC4747463
OpenAlexW2256341816

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.