Evidence map›Paper›PMID 25201220›Full record

ArticleInternational journal of oncology2014

A potential regulatory loop between Lin28B:miR‑212 in androgen-independent prostate cancer.

Emma Borrego-Diaz, Benjamin C Powers, Vugar Azizov, Scott Lovell, Ruben Reyes, Bradley Chapman, Ossama Tawfik, Douglas McGregor, Francisco J Diaz, Xinkun Wang and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in International journal of oncology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-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

18 citing papers in PubMed, 24 citations in OpenAlex.

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  9. Reports of biochemistry & molecular biology · 2019
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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

11 authors at 4 institutions in 1 country.

Emma Borrego-DiazDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
Benjamin C PowersDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
Vugar AzizovDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
Scott LovellProtein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Main Campus, Lawrence, KS 66047, USA.
Ruben ReyesDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
Bradley ChapmanDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
Ossama TawfikUniversity of Kansas Cancer Center, Kansas City, KS 66160, USA.
Douglas McGregorVeterans Administration Medical Center, Kansas City, MO 64128, USA.
Francisco J DiazUniversity of Kansas Cancer Center, Kansas City, KS 66160, USA.
Xinkun WangGenomic Facility, University of Kansas, Main Campus, Lawrence, KS 66047, USA.
Peter Van VeldhuizenDivision of Hematology/Oncology, Department of Internal Medicine, University of Kansas Medical Center, Westwood, KS 66205, USA.
University of Kansas Medical Center · USThe University of Kansas Cancer Center · USUniversity of Kansas · USUnited States Department of Veterans Affairs · US

Funding

TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI HOLYOAK, TODD · 2002 to 2011
$20.1M
Heartland Institute for Clinical and Translational ResearchUL1TR000001 · NCATS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI BAROHN, RICHARD J. · 2012 to 2015
$13.0M
Novel Approaches for the Control of Microbial PathogensP30GM103326 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 2012 to 2016
$5.3M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
NCATS NIH HHS UL1 TR000001NCATS NIH HHS UL1TR000001-02NCRR NIH HHS 5P20RR017708-10NCRR NIH HHS P20 RR017708NIGMS NIH HHS 8P20GM103420-10NIGMS NIH HHS P20 GM103420NIGMS NIH HHS P30 GM103326
6 · The paper itself

Abstract

Lin28 is a family of RNA binding proteins and microRNA regulators. Two members of this family have been identified: Lin28A and Lin28B, which are encoded by genes localized in different chromosomes but share a high degree of sequence identity. The role of Lin28B in androgen-independent prostate cancer (AIPC) is not well understood. Lin28B is expressed in all grades of prostatic carcinomas and prostate cancer cell lines, but not in normal prostate tissue. In this study we found that Lin28B co-localized in the nucleus and cytoplasm of the DU145 AIPC. The expression of Lin28B protein positively correlated with the expression of the c-Myc protein in the prostate cancer cell lines and silencing of Lin28B also correlated with a lower expression of the c-Myc protein, but not with the downregulation of c-Myc messenger RNA (mRNA) in the DU145 AIPC cells. We hypothesized that Lin28B regul-ates the expression of c-Myc protein by altering intermediate c-Myc suppressors. Therefore, a microRNA profile of DU145 cells was performed after Lin28B siRNA silencing. Nineteen microRNAs were upregulated and eleven microRNAs were downregulated. The most upregulated microRNAs were miR-212 and miR-2278. Prior reports have found that miR-212 is suppressed in prostate cancer. We then ran TargetScan software to find potential target mRNAs of miR-212 and miR-2278, and it predicted Lin28B mRNA as a potential target of miR-212, but not miR-2278. TargetScan also predicted that c-Myc mRNA is not a potential target of miR-212 or miR-2278. These observations suggest that Lin28B:miR-212 may work as a regulatory loop in androgen-independent prostate cancer. Furthermore, we report a predictive 2-fold symmetric model generated by the superposition of the Lin28A structure onto the I-TASSER model of Lin28B. This structural model of Lin28B suggests that it shows unique microRNA binding characteristics. Thus, if Lin28B were to bind miRNAs in a manner similar to Lin28A, conformational changes would be necessary to prevent steric clashes in the C-terminal and linker regions between the CSD and ZNF domains.

Indexed as

AndrogensCell Line, TumorCell ProliferationGene Expression Regulation, NeoplasticHumansMaleMicroRNAsProstatic NeoplasmsProto-Oncogene Proteins c-mycRNA-Binding ProteinsRNA, MessengerAndrogensLIN28B protein, humanMicroRNAsProto-Oncogene Proteins c-mycRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID25201220
PMCPMC4215582
OpenAlexW1996312500

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.