Evidence map›Paper›PMID 22027828›Full record

ArticleThe Journal of biological chemistry2011

Galectin-9 protein expression in endothelial cells is positively regulated by histone deacetylase 3.

Saydul Alam, Hongling Li, Andriana Margariti, Daniel Martin, Anna Zampetaki, Ouassila Habi, Gillian Cockerill, Yanhua Hu, Qingbo Xu, Lingfang Zeng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

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  14. EZH2 promotes hepatocellular carcinoma progression through modulating miR-22/galectin-9 axis.Journal of experimental & clinical cancer research : CR · 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

10 authors at 3 institutions in 1 country.

Saydul AlamCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Hongling LiCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Andriana MargaritiCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Daniel MartinCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Anna ZampetakiCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Ouassila HabiCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Gillian CockerillDepartment of Cardiovascular Science, St. George's University of London, London SW17 0RE, United Kingdom.
Yanhua HuCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Qingbo XuCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom.
Lingfang ZengCardiovascular Division, King's College London British Heart Founcation Centre, London SE5 9NU, United Kingdom. Electronic address: lingfang.zeng@kcl.ac.uk.
King's College London · GBBritish Heart Foundation · GBSt George's, University of London · GB

Funding

British Heart Foundation
6 · The paper itself

Abstract

Galectin-9 expression in endothelial cells can be induced in response to inflammation. However, the mechanism of its expression remains unclear. In this study, we found that interferon-γ (IFN-γ) induced galectin-9 expression in human endothelial cells in a time-dependent manner, which coincided with the activation of histone deacetylase (HDAC). When endothelial cells were treated with the HDAC3 inhibitor, apicidin, or shRNA-HDAC3 knockdown, IFN-γ-induced galectin-9 expression was abolished. Overexpression of HDAC3 induced the interaction between phosphoinositol 3-kinase (PI3K) and IFN response factor 3 (IRF3), leading to IRF3 phosphorylation, nuclear translocation, and galectin-9 expression. HDAC3 functioned as a scaffold protein for PI3K/IRF3 interaction. In addition to galectin-9 expression, IFN-γ also induced galectin-9 location onto plasma membrane, which was HDAC3-independent. Importantly, HDAC3 was essential for the constitutive transcription of PI3K and IRF3, which might be responsible for the basal level of galectin-9 expression. The phosphorylation of IRF3 was essential for galectin-9 expression. This study provides new evidence that HDAC3 regulates galectin-9 expression in endothelial cells via interaction with PI3K-IRF3 signal pathway.

Indexed as

Gene Expression Regulation, EnzymologicEndothelial CellsGalectinsHistone Deacetylase 3Histone DeacetylasesHumansInflammationInterferon-gammaInterferon Regulatory Factor-3InterferonsModels, BiologicalPhosphatidylinositol 3-KinasesSignal TransductionSubcellular FractionsGalectinsHistone Deacetylase 3Histone DeacetylasesInterferon-gammaInterferon Regulatory Factor-3InterferonsLGALS9 protein, humanPhosphatidylinositol 3-Kinases

Identifiers

PMID22027828
PMCPMC3243525
OpenAlexW1968809860

What OpenQuestion holds

Textmetadata
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.