Evidence map›Paper›PMID 17369847›Full record

ArticleOncogene2007

IGF-II and IGFBP-2 differentially regulate PTEN in human breast cancer cells.

C M Perks, E G Vernon, A H Rosendahl, D Tonge, J M P Holly

Abstract read
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In one paragraph

Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 7% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 167 citations in OpenAlex.

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1 more citing papers are in PubMed but not listed here.

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 4 institutions in 2 countries.

C M PerksIGF & Metabolic Endocrinology Group, Department of Clinical Sciences at North Bristol, Southmead Hospital, University of Bristol, Bristol, UK. Claire.m.perks@bristol.ac.uk
E G Vernon
A H Rosendahl
D Tonge
J M P Holly
Southmead Hospital · GBAstraZeneca (United Kingdom) · GBLund University · SEUniversity of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dual-function phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is the second most frequently mutated gene in human cancers. PTEN counteracts the functions of many growth factors, the most prevalent of which is insulin-like growth factor II (IGF-II). PTEN expression is stimulated by IGF-II forming a feedback loop. Investigating IGF-binding protein (IGFBP) modulation of IGF-II actions on MCF-7 breast cancer cells, we found that IGFBP-2 also regulates PTEN. The MCF-7 cells were not responsive to high doses of IGF-II due to induction of PTEN, which was not observed with an IGF-II-analog that does not bind to IGFBPs or in the presence of an inhibitor that prevents IGFs associating with IGFBPs. These cells predominantly produce IGFBP-2: blocking IGFBP-2 with a specific antibody, or preventing IGFBP-2 binding to integrins, restored the induction of PTEN and the cells were non-responsive to high doses of the IGF-II-analog. Our findings indicate that breast cancer cells do not respond to high doses of IGF-II due to induction of PTEN, but IGFBP-2, when free from IGF-II can suppress PTEN. Levels of IGFBP-2 are elevated frequently in human tumors: its ability to regulate PTEN could have important implications in relation to therapeutic strategies targeting growth factor pathways.

Indexed as

Gene Expression Regulation, NeoplasticBreast NeoplasmsCell Line, TumorDisease ProgressionDose-Response Relationship, DrugHumansInsulin-Like Growth Factor Binding Protein 2Insulin-Like Growth Factor IIIntegrinsIntercellular Signaling Peptides and ProteinsOligopeptidesPeptide FragmentsPTEN PhosphohydrolaseSignal TransductionSomatomedinsarginyl-glycyl-aspartic acidInsulin-Like Growth Factor Binding Protein 2Insulin-Like Growth Factor IIIntegrinsIntercellular Signaling Peptides and ProteinsOligopeptidesPeptide FragmentsPTEN PhosphohydrolasePTEN protein, humanSomatomedins

Identifiers

PMID17369847
OpenAlexW2029295641

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.