Evidence map›Paper›PMID 24163373›Full record

ArticleThe Journal of biological chemistry2013

Histone lysine-specific demethylase 1 (LSD1) protein is involved in Sal-like protein 4 (SALL4)-mediated transcriptional repression in hematopoietic stem cells.

Li Liu, Joseph Souto, Wenbin Liao, Yongping Jiang, Yangqiu Li, Ryuichi Nishinakamura, Suming Huang, Todd Rosengart, Vincent W Yang, Michael Schuster and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.9field-weighted citation impact, top 14% 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, 37 citations in OpenAlex.

  1. Article
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  8. Review
  9. Review
  10. SALL4 Oncogenic Function in Cancers: Mechanisms and Therapeutic Relevance.International journal of molecular sciences · 2022
    Review
  11. Article
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  13. Article
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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

12 authors at 6 institutions in 3 countries.

Li LiuFrom the Departments of Surgery.
Joseph Souto
Wenbin Liao
Yongping Jiang
Yangqiu Li
Ryuichi Nishinakamura
Suming Huang
Todd Rosengart
Vincent W Yang
Michael Schuster
Yupo Ma
Jianchang Yang
State University of New York · USBaylor College of Medicine · USChinese Academy of Medical Sciences & Peking Union Medical College · CNJinan University · CNKumamoto University · JPUniversity of Florida · US

Funding

A mouse model of myelodysplastic syndrome progression and leukemic stem cellsR01HL087948 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MA, YUPO · 2008 to 2012
$2.7M
Transcriptional regulation of TAL1/SCL in normal and malignant hematopoiesisR01HL090589 · NHLBI · UNIVERSITY OF FLORIDA · PI HUANG, SUMING · 2008 to 2012
$1.9M
NHLBI NIH HHS R01 HL087948NHLBI NIH HHS R01HL087948NHLBI NIH HHS R01 HL090589
6 · The paper itself

Abstract

The stem cell protein SALL4 plays a critical role in hematopoiesis by regulating the cell fate. In primitive hematopoietic precursors, it activates or represses important genes via recruitment of various epigenetic factors such as DNA methyltransferases, and histone deacylases. Here, we demonstrate that LSD1, a histone lysine demethylase, also participates in the trans-repressive effects of SALL4. Based on luciferase assays, the amine oxidase domain of LSD1 is important in suppressing SALL4-mediated reporter transcription. In freshly isolated adult mouse bone marrows, both SALL4 and LSD1 proteins are preferentially expressed in undifferentiated progenitor cells and co-localize in the nuclei. Further sequential chromatin immunoprecipitation assay confirmed that these two factors share the same binding sites at the promoter regions of important hematopoietic regulatory genes including EBF1, GATA1, and TNF. In addition, studies from both gain- and loss-of-function models revealed that SALL4 dynamically controls the binding levels of LSD1, which is accompanied by a reversely changed histone 3 dimethylated lysine 4 at the same promoter regions. Finally, shRNA-mediated knockdown of LSD1 in hematopoietic precursor cells resulted in altered SALL4 downstream gene expression and increased cellular activity. Thus, our data revealed that histone demethylase LSD1 may negatively regulate SALL4-mediated transcription, and the dynamic regulation of SALL4-associated epigenetic factors cooperatively modulates early hematopoietic precursor proliferation.

Indexed as

AnimalsBasic Helix-Loop-Helix ProteinsBinding SitesBone Marrow CellsCell ProliferationCells, CulturedDNA-Binding ProteinsDNA Modification MethylasesEpigenesis, GeneticGene SilencingHematopoiesisHematopoietic Stem CellsHistone DemethylasesHistonesLysineMiceBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsDNA Modification MethylasesHistone DemethylasesHistonesKDM1a protein, mouseLysineOxidoreductases, N-DemethylatingProto-Oncogene ProteinsSall4 protein, mouseTAL1 protein, humanT-Cell Acute Lymphocytic Leukemia Protein 1Transcription FactorsBone MarrowDNA MethylationHematopoiesisHematopoietic ProgenitorHistone DemethylationMi-2·NuRD ComplexRepressor ProteinSALL FamilyStem Cells

Identifiers

PMID24163373
PMCPMC3843083
OpenAlexW2005300267

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.