Evidence map›Paper›PMID 20100838›Full record

ArticleThe Journal of biological chemistry2010

Promyelocytic leukemia protein controls cell migration in response to hydrogen peroxide and insulin-like growth factor-1.

Erin L Reineke, Yu Liu, Hung-Ying Kao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
1.5field-weighted citation impact, top 19% 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, 40 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The roles of KLHL family members in human cancers.American journal of cancer research · 2022
    Review
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  19. Article
  20. The role of PML ubiquitination in human malignancies.Journal of biomedical science · 2012
    Review
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

3 authors at 1 institution in 1 country.

Erin L ReinekeDepartment of Biochemistry, School of Medicine, Case Western Reserve University, the Case Comprehensive Cancer Center, and University Hospitals of Cleveland, Cleveland, Ohio 44106.
Yu LiuDepartment of Biochemistry, School of Medicine, Case Western Reserve University, the Case Comprehensive Cancer Center, and University Hospitals of Cleveland, Cleveland, Ohio 44106.
Hung-Ying KaoDepartment of Biochemistry, School of Medicine, Case Western Reserve University, the Case Comprehensive Cancer Center, and University Hospitals of Cleveland, Cleveland, Ohio 44106. Electronic address: hxk43@cwru.edu.
University Hospitals of Cleveland · US

Funding

Aging-Cancer Research Program Development at CWRU CCCP20CA103736 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI BERGER, NATHAN A. · 2003 to 2007
$3.8M
Alpha actinin 4: its functions and regulationR01DK078965 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI KAO, HUNG-YING · 2009 to 2013
$1.7M
Histone deacetylase 7 and its interacting proteins in endothelial cellsR01HL093269 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI KAO, HUNG-YING · 2010 to 2013
$1.5M
NCI NIH HHS P20 CA103736NHLBI NIH HHS HL093269NHLBI NIH HHS R01 HL093269NIDDK NIH HHS R01 DK078965
6 · The paper itself

Abstract

Promyelocytic leukemia protein (PML) was originally identified as part of a chromosomal translocation that contributes to the development of acute promyelocytic leukemia (APL). Since its discovery, PML has been found to play diverse roles in different cellular processes. Notably, PML has anti-proliferative and pro-apoptotic activity that supports its role as a tumor suppressor. We have previously shown that the peptidyl-prolyl isomerase Pin1 is able to affect cell proliferation and hydrogen peroxide (H(2)O(2))-mediated cell death through modulation of the steady-state levels of PML. We have extended these studies to show that the interaction between PML and Pin1 is targeted by multiple extracellular signals in the cell. We show that H(2)O(2) up-regulates and IGF-1 down-regulates PML expression in a Pin1-dependent manner. Interestingly, we found that H(2)O(2)- and IGF-1-mediated alteration in PML accumulation regulate MDA-MB-231 cell migration. Furthermore, we show that the control of cell migration by PML, and thus H(2)O(2) and IGF-1, results from PML-dependent decreased expression of integrin beta1 (ITGB1). Knockdown of Pin1 leads to decreased cell migration, lower levels of ITGB1 expression and resistance to IGF-1- and H(2)O(2)-induced changes in cell migration and ITGB1 expression. Taken together, our work identifies PML as a common target for H(2)O(2) and IGF-1 and supports a novel tumor suppressive role for PML in controlling cell migration through the expression of ITGB1.

Indexed as

Gene Expression Regulation, LeukemicCell Line, TumorCell MovementDown-RegulationHumansHydrogen PeroxideInsulin-Like Growth Factor IIntegrin beta1Leukemia, Promyelocytic, AcuteMicroscopy, FluorescenceNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePlasmidsRNA, Small InterferingTime FactorsWound HealingHydrogen PeroxideInsulin-Like Growth Factor IIntegrin beta1NIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanRNA, Small Interfering

Identifiers

PMID20100838
PMCPMC2843199
OpenAlexW1976919956

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.