Evidence map›Paper›PMID 27022024›Full record

ArticleThe Journal of biological chemistry2016

Modeling the Etiology of p53-mutated Cancer Cells.

Ricardo E Perez, Hong Shen, Lei Duan, Reuben H Kim, Terresa Kim, No-Hee Park, Carl G Maki

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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

7 authors.

Ricardo E PerezFrom the Department of Anatomy and Cell Biology, Rush University Medical Center, Chicago, Illinois 60612 and.
Hong ShenFrom the Department of Anatomy and Cell Biology, Rush University Medical Center, Chicago, Illinois 60612 and.
Lei DuanFrom the Department of Anatomy and Cell Biology, Rush University Medical Center, Chicago, Illinois 60612 and.
Reuben H KimThe Shapiro Family Laboratory of Viral Oncology and Aging Research, UCLA School of Dentistry and David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
Terresa KimThe Shapiro Family Laboratory of Viral Oncology and Aging Research, UCLA School of Dentistry and David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
No-Hee ParkThe Shapiro Family Laboratory of Viral Oncology and Aging Research, UCLA School of Dentistry and David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
Carl G MakiFrom the Department of Anatomy and Cell Biology, Rush University Medical Center, Chicago, Illinois 60612 and carl_maki@rush.edu.

Funding

Epigenetic Control of HPV-associated Oral CarcinogenesisR01DE023874 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KIM, REUBEN HAN-KYU, WANG, CUN-YU · 2013 to 2017
$2.3M
Cellular Responses to p53 Activation by Nutlin-3aR01CA137598 · NCI · RUSH UNIVERSITY MEDICAL CENTER · PI MAKI, CARL G · 2009 to 2013
$1.5M
Modeling The Etiology of P53 Mutated Cancer CellsR21CA178733 · NCI · RUSH UNIVERSITY MEDICAL CENTER · PI MAKI, CARL G · 2013 to 2014
$379k
NCI NIH HHS R01 CA137598NCI NIH HHS R21 CA178733NIDCR NIH HHS R01 DE023874
6 · The paper itself

Abstract

p53 gene mutations are among the most common alterations in cancer. In most cases, missense mutations in one TP53 allele are followed by loss-of-heterozygosity (LOH), so tumors express only mutant p53. TP53 mutations and LOH have been linked, in many cases, with poor therapy response and worse outcome. Despite this, remarkably little is known about how TP53 point mutations are acquired, how LOH occurs, or the cells involved. Nutlin-3a occupies the p53-binding site in MDM2 and blocks p53-MDM2 interaction, resulting in the stabilization and activation of p53 and subsequent growth arrest or apoptosis. We leveraged the powerful growth inhibitory activity of Nutlin-3a to select p53-mutated cells and examined how TP53 mutations arise and how the remaining wild-type allele is lost or inactivated. Mismatch repair (MMR)-deficient colorectal cancer cells formed heterozygote (p53 wild-type/mutant) colonies when cultured in low doses of Nutlin-3a, whereas MMR-corrected counterparts did not. Placing these heterozygotes in higher Nutlin-3a doses selected clones in which the remaining wild-type TP53 was silenced. Our data suggest silencing occurred through a novel mechanism that does not involve DNA methylation, histone methylation, or histone deacetylation. These data indicate MMR deficiency in colorectal cancer can give rise to initiating TP53 mutations and that TP53 silencing occurs via a copy-neutral mechanism. Moreover, the data highlight the use of MDM2 antagonists as tools to study mechanisms of TP53 mutation acquisition and wild-type allele loss or silencing in cells with defined genetic backgrounds.

Indexed as

Colorectal NeoplasmsDNA MethylationDNA Mismatch RepairLoss of HeterozygosityModels, BiologicalProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53AnimalsCell Line, TumorHumansImidazolesPiperazinesImidazolesMDM2 protein, humannutlin 3PiperazinesProto-Oncogene Proteins c-mdm2TP53 protein, humanTumor Suppressor Protein p53cancercancer biologymutagenesis in vitrop53tumor suppressor gene

Identifiers

PMID27022024
PMCPMC4858965

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.