Evidence map›Paper›PMID 10208431›Full record

ArticleOncogene1999

The t(8;21) fusion protein, AML1/ETO, transforms NIH3T3 cells and activates AP-1.

R C Frank, X Sun, F J Berguido, A Jakubowiak, S D Nimer

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-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

27 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  11. AML1-ETO fusion protein up-regulates TRKA mRNA expression in human CD34+ cells, allowing nerve growth factor-induced expansion.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  12. AML1-ETO and C-KIT mutation/overexpression in t(8;21) leukemia: implication in stepwise leukemogenesis and response to Gleevec.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
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  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

5 authors at 2 institutions in 1 country.

R C FrankSloan Kettering Institute, Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
X Sun
F J Berguido
A Jakubowiak
S D Nimer
Kettering University · USMemorial Sloan Kettering Cancer Center · US

Funding

Investigational Cancer Therapeutics Training Program (ICTTP)T32CA009207 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Omar Abdel-Wahab, Alexander Drilon · 1985 to 2026
$13.7M
AML1/ETO FUSION PROTEIN AND LEUKEMOGENESISK08CA070388 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI FRANK, RICHARD C · 1996 to 2000
$91k
MOLECULAR PATHOGENESIS OF MYELOID LEUKEMIAR01DK043025 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI NIMER, STEPHEN DAVID · 1990 to 1999
–
NCI NIH HHS CA09207NCI NIH HHS K08 CA70388NIDDK NIH HHS DK 43025
6 · The paper itself

Abstract

The 8;21 translocation is the most common cytogenetic abnormality in human acute myelogenous leukemia, joining the AML1 gene on chromosome 21, to the ETO gene on chromosome 8, forming the AML1/ETO fusion gene. The AMLI/ETO fusion protein has been shown to function mainly as a transcriptional repressor of AML1 target genes and to block AML1 function in vitro and in vivo. However, AML1/ETO can also activate the BCL-2 promoter and cause enhanced hematopoietic progenitor self-renewal in vitro, suggesting gain-of-functions unique to the fusion protein. We used NIH3T3 cells to determine the transforming capacity of AML1/ETO, and to further characterize its mechanism of action. Expression of AML1/ETO in NIH3T3 cells caused cell-type specific cell death, and cellular transformation, characterized by phenotypic changes, anchorage-independent growth, and tumor formation in nude mice. In contrast, neither expression of AML1A, AML1B or ETO altered the normal growth pattern of the cells. To investigate the mechanism of transformation by AML1/ETO, we analysed the levels of activated, phosphorylated c-Jun (ser63) and other constituents of the AP-1 complex, in the presence of various AML1/ETO related proteins. Expression of AML1/ETO increased the level of c-Jun-P (ser63), and activated AP-1 dependent transcription, which was inhibited by expression of a dominant-negative c-Jun protein. Mutational analysis revealed that the runt homology domain (RHD) and a C-terminal transcriptional repression domain in AML1/ETO are required for transformation, activation of c-Jun and increased AP-1 activity. These results establish the transforming potential of the t(8;21) fusion protein and link this gain-of-function property to modulation of AP-1 activity.

Indexed as

Chromosomes, Human, Pair 21Chromosomes, Human, Pair 8Oncogene Proteins, FusionProto-Oncogene ProteinsTranslocation, Genetic3T3 CellsAnimalsCell DivisionCell Transformation, NeoplasticCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsGene ExpressionHumansMicePhosphorylationProto-Oncogene Proteins c-junAML1-ETO fusion protein, humanCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsOncogene Proteins, FusionProto-Oncogene ProteinsProto-Oncogene Proteins c-junRecombinant Fusion ProteinsRUNX1 protein, humanRunx1 protein, mouseRUNX1T1 protein, humanRUNX1 Translocation Partner 1 ProteinTranscription Factor AP-1Transcription Factors

Identifiers

PMID10208431
OpenAlexW1980771751

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.